Anatomy & Physiology Test #2 2024 PDF

WELCOME TO Anatomy & Physiology 101-127-AB 00001 Anatomy & Physiology for Paramedics I © Samuel Richer 2024 Meet your instructor ! → Pronouns: He/Him → E-mail:...

WELCOME TO Anatomy & Physiology 101-127-AB 00001 Anatomy & Physiology for Paramedics I © Samuel Richer 2024 Meet your instructor ! → Pronouns: He/Him → E-mail: [email protected] → Office: AME-308 → Office Hours: Monday: 10:30-14:30 Tuesday: 14:00-16:00 Thursday: 12:30-14:30 → How can I reach Sam: o Office hours DEC Health Science Dawson (2015-2017) o MIO o Anytime for an appointment on BSc. Physiology McGill (2017-2020) - Microsoft Teams MSc. Neuroscience McGill (2021-2024) - Zoom call Course Outline UNIT I - Characteristics of Living Things - Homeostasis UNIT II - Biomolecules & Cell Anatomy - Tissues UNIT III - Neural Transmission & the Nervous System Anonymous Feedback Form This is a place where you can submit feedback on your “Anatomy & Physiology" teacher, Samuel Richer, completely anonymously! Please feel free to give him constructive feedback on his teaching style, lecture slides, assignments and tests, etc. → Does Sam talk too fast in lecture? → Are lectures too boring? → Would you like more/fewer interactive activities? This is where you can have your voice be heard anytime throughout the semester. Link: https://forms.gle/owpTi9TrhJZBxKpK7 LE CTURE 1 Hierarchy 1 Classification of Substances (atoms, ions, molecules) 101-127-AB 00001 Anatomy & Physiology for Paramedics I © Samuel Richer 2024 (adapted from Roxane Millette) Lecture 1: Learning Objectives 1. Define each of the following levels of structural organization that make up the human body: ❑ atoms, molecules, organelles, cells, tissues, organs and systems. 2. Distinguish between: ❑ An atom ❑ A molecule ❑ An ion 3. Distinguish between ions in solutions according to experimental data (conducts electricity & mixes with water) and electron behavior (transfer or sharing electrons). 4. Describe the functional importance of ions and molecules in the human body. List the elements that make up almost all living tissues. Name & write the symbols for the major ions present inside tissue cells & between tissue cells. 5. Distinguish between ❑ Intermolecular forces ❑ Intramolecular forces ❑ Ionic Bonds ❑ Polar Covalent Bond ❑ Non-Polar Covalent Bond 6. Distinguish between hydrophilic (covalent polar) and hydrophobic (covalent non-polar) biomolecules according to experimental data (mixing with water) and electron behavior (equal sharing or unequal sharing of electrons), based on their chemical and structural formulas. Lecture 1: Atoms, Ions & Molecules LABORATORY ❑ Preparation for Spinal Cord Lab Laboratory: ❑ Pre-Lab H5P THEORY ❑ Quiz next class Wednesday October 9th ❑ Class Test Unit 1: Wednesday October 16th Why are we learning about Chemistry? This is an ANATOMY course!? 1. Hierarchy of Living Organisms Atoms are the smallest unit of an element that still maintains the property of that element. 1. Hierarchy of Living Organisms Atoms are the smallest unit of an element that still maintains the property of that element. M-o-l-e-c-u-l-e-s: Two or more atoms held together by bonds where electrons are given or shared amongst themselves. 1. Hierarchy of Living Organisms Atoms are the smallest unit of an element that still maintains the property of that element. M-o-l-e-c-u-l-e-s: Two or more atoms held together by bonds where electrons are given or shared amongst themselves. M-o-l-e-c-u-l-e-s are made of Atoms 1. Hierarchy of Living Organisms Atoms are the smallest unit of an element that still maintains the property of that element. M-o-l-e-c-u-l-e-s: Two or more atoms held together by bonds where electrons are given or shared amongst themselves. Important molecules we will learn about: Where can we find these in our bodies? 1. Hierarchy of Living Organisms Atoms are the smallest unit of an element that still maintains the property of that element. M-o-l-e-c-u-l-e-s: Two or more atoms held together by bonds where electrons are given or shared amongst themselves. These M-o-l-e-c-u-l-e-s then form ORGANELLES (parts of the cell) Ex: mitochondria, nucleus etc. 1. Hierarchy of Living Organisms Atoms are the smallest unit of an element that still maintains the property of that element. M-o-l-e-c-u-l-e-s: Two or more atoms held together by bonds where electrons are given or shared amongst themselves. These M-o-l-e-c-u-l-e-s then form ORGANELLES (parts of the cell) Ex: mitochondria, nucleus etc. ORGANELLES create a C E L L which acts like a small city. o Nucleus: parliament making decisions o Cell membrane: boarder control o Mitochondria: energy powerplant The CELL is the BASIC UNIT OF LIFE 1. Hierarchy of Living Organisms Atoms are the smallest unit of an element that still maintains the property of that element. M-o-l-e-c-u-l-e-s: Two or more atoms held together by bonds where electrons are given or shared amongst themselves. These M-o-l-e-c-u-l-e-s then form ORGANELLES (parts of the cell) Ex: mitochondria, nucleus etc. ORGANELLES create a C E L L which acts like a small city. Groups of CE L LS with similar function come together to form a TISSUE 1. Hierarchy of Living Organisms Atoms are the smallest unit of an element that still maintains the property of that element. M-o-l-e-c-u-l-e-s: Two or more atoms held together by bonds where electrons are given or shared amongst themselves. These M-o-l-e-c-u-l-e-s then form ORGANELLES (parts of the cell) Ex: mitochondria, nucleus etc. ORGANELLES create a C E L L which acts like a small city. Groups of CE L LS with similar function come together to form a TISSUE ORGANS are formed by two or more types of TISSUES that work together to complete a specific task 1. Hierarchy of Living Organisms Atoms are the smallest unit of an element that still maintains the property of that element. M-o-l-e-c-u-l-e-s: Two or more atoms held together by bonds where electrons are given or shared amongst themselves. These M-o-l-e-c-u-l-e-s then form ORGANELLES (parts of the cell) Ex: mitochondria, nucleus etc. ORGANELLES create a C E L L which acts like a small city. Groups of CE L LS with similar function come together to form a TISSUE ORGANS are formed by two or more types of TISSUES that work together to complete a specific task An ORGAN SYSTEM is a group of organs that carry out more generalized sets of functions. 1. Hierarchy of Living Organisms 8. ORGAN SYSTEMS function together to form an ORGANISM 1. Hierarchy of Living Organisms Example: Urinary System Lecture 1: Learning Objectives 1. Define each of the following levels of structural organization that make up the human body: ❑ atoms, molecules, organelles, cells, tissues, organs and systems. 2. Distinguish between: ❑ An atom ❑ A molecule ❑ An ion 3. Distinguish between ions in solutions according to experimental data (conducts electricity & mixes with water) and electron behavior (transfer or sharing electrons). 4. Describe the functional importance of ions and molecules in the human body. List the elements that make up almost all living tissues. Name & write the symbols for the major ions present inside tissue cells & between tissue cells. 5. Distinguish between ❑ Intermolecular forces ❑ Intramolecular forces ❑ Ionic Bonds ❑ Polar Covalent Bond ❑ Non-Polar Covalent Bond 6. Distinguish between hydrophilic (covalent polar) and hydrophobic (covalent non-polar) biomolecules according to experimental data (mixing with water) and electron behavior (equal sharing or unequal sharing of electrons), based on their chemical and structural formulas. 2. Atoms, Molecules, Ions The atom’s nucleus contains o Positively charged PROTONS - Nucleus o Neutral NEUTRONS - - - Around the nucleus, we have - o Negatively charged ELECTRONS - - orbiting the dense nucleus 2. Atoms, Molecules, Ions The atom’s nucleus contains o Positively charged PROTONS - Nucleus o Neutral NEUTRONS - Atom - - Around the nucleus, we have - o negatively charged ELECTRONS - - orbiting the dense nucleus How do electrons not float away ? 2. Atoms, Molecules, Ions The universal laws of electrostatics: opposite charges attract each other - - - - - - 2. Atoms, Molecules, Ions - The # of protons (p+), electrons (e-) & neutrons (n0) in an atom are different, depending on the element you are looking at. Because of this, each atom has a unique name, mass and size. 2. Atoms, Molecules, Ions The ATOMIC NUMBER in the periodic table is the number of protons (+) in the atom and is most of the time the # of electrons (-) (unless the atom is sharing or giving their electrons away) 1 proton (+) 8 protons (+) 11 protons (+) - 1 electron (-) 8 electrons (-) - - 11 electrons (-) Lecture 1: Learning Objectives 1. Define each of the following levels of structural organization that make up the human body: ❑ atoms, molecules, organelles, cells, tissues, organs and systems. 2. Distinguish between: ❑ An atom ❑ A molecule ❑ An ion 3. Distinguish between ions in solutions according to experimental data (conducts electricity & mixes with water) and electron behavior (transfer or sharing electrons). 4. Describe the functional importance of ions and molecules in the human body. List the elements that make up almost all living tissues. Name & write the symbols for the major ions present inside tissue cells & between tissue cells. 5. Distinguish between ❑ Intermolecular forces ❑ Intramolecular forces ❑ Ionic Bonds ❑ Polar Covalent Bond ❑ Non-Polar Covalent Bond 6. Distinguish between hydrophilic (covalent polar) and hydrophobic (covalent non-polar) biomolecules according to experimental data (mixing with water) and electron behavior (equal sharing or unequal sharing of electrons), based on their chemical and structural formulas. 2. Atoms, Molecules, Ions A chemical reaction occurs when 2 or more elements combine to form a Molecule, and an entirely new substance results. H2O: transparent, unreactive liquid Hydrogen: clear odourless, highly reactive gas Oxygen: clear odourless, highly reactive gas Lecture 1: Learning Objectives 1. Define each of the following levels of structural organization that make up the human body: ❑ atoms, molecules, organelles, cells, tissues, organs and systems. 2. Distinguish between: ❑ An atom ❑ A molecule ❑ An ion 3. Distinguish between ions in solutions according to experimental data (conducts electricity & mixes with water) and electron behavior (transfer or sharing electrons). 4. Describe the functional importance of ions and molecules in the human body. List the elements that make up almost all living tissues. Name & write the symbols for the major ions present inside tissue cells & between tissue cells. 5. Distinguish between ❑ Intermolecular forces ❑ Intramolecular forces ❑ Ionic Bonds ❑ Polar Covalent Bond ❑ Non-Polar Covalent Bond 6. Distinguish between hydrophilic (covalent polar) and hydrophobic (covalent non-polar) biomolecules according to experimental data (mixing with water) and electron behavior (equal sharing or unequal sharing of electrons), based on their chemical and structural formulas. 2. Atoms, Molecules, Ions 11Na 17Cl 11 + protons 17 + protons 11 - electrons 17 - electrons Net charge: _____ Net charge: _____ Na + 11 Cl - 11 protons 11 neutrons 11Na + 10 electrons 17 Cl 17 - 11 + protons 17 + protons 10 - electrons 18 - electrons Net charge: _____ Net charge: _____ If 1 atom is much more successful at attracting electrons, both atoms become charged IONS. 2. Atoms, Molecules, Ions 11Na 17Cl 11 + protons 17 + protons 11 - electrons 17 - electrons Net charge: _____ Net charge: _____ Na + 11 Cl - 11 protons 11 neutrons 11Na + 10 electrons 17 Cl 17 - 11 + protons 17 + protons 10 - electrons 18 - electrons Net charge: _____ Net charge: _____ If 1 atom is much more successful at attracting electrons, both atoms become charged IONS. 2. Atoms, Molecules, Ions 11Na 17Cl 11 + protons 17 + protons 11 - electrons 17 - electrons Net charge: _____ Net charge: _____ Na + 11 Cl - 11 protons 11 neutrons 11Na + 10 electrons 17 Cl 17 - 11 + protons 17 + protons 10 - electrons 18 - electrons Net charge: _____ Net charge: _____ 2. Atoms, Molecules, Ions 11Na 17Cl 11 + protons 17 + protons 11 - electrons 17 - electrons Net charge: _____ Net charge: _____ This is an atom This is an atom of sodium (Na) of chlorine (Cl) If 1 atom is much more successful at + attracting electrons, both atoms 11 Na become charged ions. Cl - 11 protons 11 neutrons 11Na + 10 electrons 17 Cl 17 - 11 + protons 17 + protons 10 - electrons 18 - electrons Net charge: _____ Net charge: _____ This is an ion of sodium (Na+) This is an ion of chlorine (Cl-) 2. Atoms, Molecules, Ions If 1 atom is much more successful at attracting electrons, both atoms become charged ions. Lecture 1: Learning Objectives 1. Define each of the following levels of structural organization that make up the human body: ❑ atoms, molecules, organelles, cells, tissues, organs and systems. 2. Distinguish between: ❑ An atom ❑ A molecule ❑ An ion 3. Distinguish between ions in solutions according to experimental data (conducts electricity & mixes with water) and electron behavior (transfer or sharing electrons). 4. Describe the functional importance of ions and molecules in the human body. List the elements that make up almost all living tissues. Name & write the symbols for the major ions present inside tissue cells & between tissue cells. 5. Distinguish between ❑ Intermolecular forces ❑ Intramolecular forces ❑ Ionic Bonds ❑ Polar Covalent Bond ❑ Non-Polar Covalent Bond 6. Distinguish between hydrophilic (covalent polar) and hydrophobic (covalent non-polar) biomolecules according to experimental data (mixing with water) and electron behavior (equal sharing or unequal sharing of electrons), based on their chemical and structural formulas. 3. Ions in solution and conduction Electricity is the movement of charges. IONS are charged and can produce electricity Cl- Na+ Na+ Cl- Cl- Na+ H2O C6H12O6 Na+ & Cl- (water) (glucose/sugar) (from NaCl salt) Not an ION Not an ION Is an ION cannot conduct cannot conduct can conduct Lecture 1: Learning Objectives 1. Define each of the following levels of structural organization that make up the human body: ❑ atoms, molecules, organelles, cells, tissues, organs and systems. 2. Distinguish between: ❑ An atom ❑ A molecule ❑ An ion 3. Distinguish between ions in solutions according to experimental data (conducts electricity & mixes with water) and electron behavior (transfer or sharing electrons). 4. Describe the functional importance of ions and molecules in the human body. List the elements that make up almost all living tissues. Name & write the symbols for the major ions present inside tissue cells & between tissue cells. 5. Distinguish between ❑ Intermolecular forces ❑ Intramolecular forces ❑ Ionic Bonds ❑ Polar Covalent Bond ❑ Non-Polar Covalent Bond 6. Distinguish between hydrophilic (covalent polar) and hydrophobic (covalent non-polar) biomolecules according to experimental data (mixing with water) and electron behavior (equal sharing or unequal sharing of electrons), based on their chemical and structural formulas. 4. Ions & Molecules in the body Extracellular fluid Na+ Plasma membrane K+ K+ Na+ Na+ Na+ K+ Na+ K+ K+ K+ Na+ K+ K+ Na+ Na+ K+ Intracellular fluid Na+ K+ Na+ Na+ K+ Na+ K+ K+ K+ Na+ Na+ Na+ Na+ Na+ K+ K+ K+ Na+ Na+ Na+ Na+ [K+] [Na+] Extracellular Low [K+] High [Na+] fluid Intracellular High [K+] Low [Na+] fluid  4. Ions & Molecules in the body In our bodies, nervous signals are produced by the movement of ions (Na+, K+) Na+ Na+ Na+ Na+ Na+ Na+ K+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ K+ K+ Na + Na+ K+ Na+ Na+ K+ Na+ K+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ K+ K+ Na+ Na+ K+ K+ K+ K+ Na+ Na+ Na+ K+ K+ Na+ Na+ Na+ Na+ K+ Na+ Na+ K+ Na+ K+ K+ Na + K + K+ K + Na+ K+ Na+ K+ K + K+ Na + K + K+ K+ K+ Na+ K+ K+ Na+ Na+ K+ Na+ Na+ Na+ K+ K+ K+ K + Na+ Na+ Na+ Na+ K+ K+ K+ K+ Na+ K+ Na+ Na+ Na+ Na+ K+ K+ Na+ K+ K+ Na+ K+ Na+ K+ K + K + K+ K+ Na + Na+ Na + K+ K+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ K + Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na + Na+ Na+ Na+ Na+ Na+ Na+ Na + Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na + Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na+ Na + Na+ Na+ Resting Neuron Na+ Rushes in Active Neuron the neuron 4. Ions & Molecules in the body In our bodies, nervous signals are produced by the movement of ions (Na+, K+) 4. Ions & Molecules in the body Lecture 1: Learning Objectives 1. Define each of the following levels of structural organization that make up the human body: ❑ atoms, molecules, organelles, cells, tissues, organs and systems. 2. Distinguish between: ❑ An atom ❑ A molecule ❑ An ion 3. Distinguish between ions in solutions according to experimental data (conducts electricity & mixes with water) and electron behavior (transfer or sharing electrons). 4. Describe the functional importance of ions and molecules in the human body. List the elements that make up almost all living tissues. Name & write the symbols for the major ions present inside tissue cells & between tissue cells. 5. Distinguish between ❑ Intermolecular forces ❑ Intramolecular forces ❑ Ionic Bonds ❑ Polar Covalent Bond ❑ Non-Polar Covalent Bond 6. Distinguish between hydrophilic (covalent polar) and hydrophobic (covalent non-polar) biomolecules according to experimental data (mixing with water) and electron behavior (equal sharing or unequal sharing of electrons), based on their chemical and structural formulas. 5. Chemical Bonds Bonds can be… attractions between two attractions between two or more Atoms or more M-o-l-e-c-u-l-e-s Lecture 1: Learning Objectives 1. Define each of the following levels of structural organization that make up the human body: ❑ atoms, molecules, organelles, cells, tissues, organs and systems. 2. Distinguish between: ❑ An atom ❑ A molecule ❑ An ion 3. Distinguish between ions in solutions according to experimental data (conducts electricity & mixes with water) and electron behavior (transfer or sharing electrons). 4. Describe the functional importance of ions and molecules in the human body. List the elements that make up almost all living tissues. Name & write the symbols for the major ions present inside tissue cells & between tissue cells. 5. Distinguish between ❑ Intermolecular forces ❑ Intramolecular forces ❑ Ionic Bonds ❑ Polar Covalent Bond ❑ Non-Polar Covalent Bond 6. Distinguish between hydrophilic (covalent polar) and hydrophobic (covalent non-polar) biomolecules according to experimental data (mixing with water) and electron behavior (equal sharing or unequal sharing of electrons), based on their chemical and structural formulas. 5. Chemical Bonds Bonds can be… IONIC BONDS COVALENT BONDS (transfer of electrons) (sharing of electrons) − 𝛿 + 𝛿 Cl- Na+ e- POLAR COVALENT NON-POLAR COVALENT with electrons “stolen” & electrons shared unequally electrons shared equally transferred from one atom to pulled more to 1 atom Atoms are equally pulling the other creating a partial charge + positive pole (𝛿 ) & negative pole (𝛿-) 5. Chemical Bonds How do we determine whether Bonds can be… 2 atoms form an: ionic bond polar covalent bond or Cl- non-polar covalent? Na+ e- with electrons “stolen” and with electrons with electrons transferred from one atom shared unequally and shared equally Electronegativity to the other pulled more to one side I O N I C (transfer of electrons) C O V A L E N T (sharing of electrons) of the two atoms Between Metal & Non-Metal Between Non-Metal & Non-Metal 5. Chemical Bonds The ability for an atom to attract electrons from another atom Electronegativity  Electronegativity Values High electronegativity # = strong attraction for electrons in other atoms Low electronegativity # = low attraction for electrons in other atoms If the difference in electron attraction between the atoms is: 0 - 0.4 nonpolar covalent (hydrophobic): lipids, usually C & H 0.5 - 1.7 polar covalent (hydrophilic): interact with water but do not conduct electricity, usually N & O 1.8- 4.0 ionic: interact with water & conduct electricity, usually Na +, K+ & Cl- 5. Chemical Bonds Polarity is the distribution of electrons in a bond In NON-POLAR COVALENT bonds, the electron pairs are shared equally because the 2 atoms are equally similar in electronegativity. − 𝛿 In a POLAR COVALENT BONDS, electron pairs are not shared equally 1 atom is more electronegative than the other + 𝛿 + 𝛿 Unequal sharing of electrons causes a partial + − positive pole 𝛿 and partial negative pole 𝛿 for each atom. The more electronegative an atom, the more strongly it pulls shared electrons toward itself. 5. Chemical Bonds Bonds are attractions between two or more Atoms or M-o-l-e-c-u-l-e-s o Bonds are not magic sticks (-) here! Intra-molecular forces (within the molecule) Ionic bonds Polar covalent bond Non-Polar covalent bond Complete transfer of electrons Electrons are shared unequally Electrons are shared equally Full charges on atoms Partial charges on atoms No charges on atoms Intermolecular forces (between 2 molecules) Hydrogen bonds Lecture 1: Learning Objectives 1. Define each of the following levels of structural organization that make up the human body: ❑ atoms, molecules, organelles, cells, tissues, organs and systems. 2. Distinguish between: ❑ An atom ❑ A molecule ❑ An ion 3. Distinguish between ions in solutions according to experimental data (conducts electricity & mixes with water) and electron behavior (transfer or sharing electrons). 4. Describe the functional importance of ions and molecules in the human body. List the elements that make up almost all living tissues. Name & write the symbols for the major ions present inside tissue cells & between tissue cells. 5. Distinguish between ❑ Intermolecular forces ❑ Intramolecular forces ❑ Ionic Bonds ❑ Polar Covalent Bond ❑ Non-Polar Covalent Bond 6. Distinguish between hydrophilic (covalent polar) and hydrophobic (covalent non-polar) biomolecules according to experimental data (mixing with water) and electron behavior (equal sharing or unequal sharing of electrons), based on their chemical and structural formulas. 6. Hydrophilic & Hydrophobic Water (H2O) is a POLAR COVALENT MOLECULE since o part of the molecule is slightly positive  + o part of the molecule is slightly negative  - + 𝛿 + 𝛿 + + 𝛿 𝛿 6. Hydrophilic & Hydrophobic The polar nature of water makes it very important because this polarity allows water to form intermolecular Hydrogen-bonds between water molecules 6. Hydrophilic & Hydrophobic As a polar molecule, water can dissolve any other polar substance (anything with a charge or partial charge) Water can dissolve: Small Ionic compounds into separate Large polar compounds ions surrounded by H2O molecules. are similarly dissolved. 6. Hydrophilic & Hydrophobic HYDROPHILIC HYDROPHOBIC Water Loving Water Fearing 🫣 Compounds that are polar dissolve in Compounds that are non-polar DON’T water which is also polar dissolve in water which is a polar substance These compounds are considered These compounds are considered hydrophilic (water-loving ) hydrophobic (water-fearing 🫣 ) LE CTURE 2 Biomolecules Carbohydrates Proteins Lipids Nucleic Acids 101-127-AB 00001 Anatomy & Physiology for Paramedics I © Samuel Richer 2024 (adapted from Roxane Millette & Jason ) Announcements LABORATORY → Post-Lab complete the PDF due Friday October 25th → Read Lab Manual for tissues lab → Pre-Lab (2 separate H5P) ❑ Prelab 4 week 2: tissue layers and epithelium H5P ❑ Prelab 4 week 2: connective tissue H5P THEORY → Assignment Problem set 1 & 2 (due before Unit Test 2) Tutors for Peer-Tutoring Program $$$ Lecture 2: Learning Objectives 1. Describe biomolecules. 2. Describe the structure and function of each class of biomolecule 1. Identification of molecules (just from chemical formula, structural formula and/or by shape) 2. Know in what food those biomolecules (nutrients) are available 3. Know in what parts of the cell/ cell organelles each biomolecule plays a role 3. Define monomer, intermediate, polymer and identify 1. carbohydrate: 1. monomer/monosaccharides: glucose/galactose, fructose, glycerol 2. intermediates/disaccharides: sucrose, maltose, lactose 3. polymers/polysaccharides: (starch, cellulose/fiber, glycogen) 2. protein: 1. monomer: amino acid, 2. intermediate : peptide/amino acid sequence 3. polymer : protein (the difference between globular proteins & fibrous proteins will be emphasized later on) 3. lipid: 1. monomer: fatty acid (saturated vs unsaturated), glycerol 2. polymer: triglyceride/fat, phospholipid, steroids. 4. Describe the functional importance of each of the biomolecules in the human body. 5. Describe which metabolic imbalances (hyperthermia and acidosis) can denature proteins and state its medical importance. Biomolecules Biomolecules The cells of living things are made up of 4 classes of large biomolecules LIPIDS NUCLEIC ACIDS CARBOHYDRATES PROTEINS Make up Encodes & transmits Provides a source of 1. pores/pumps for transport cell membranes genetic information energy to the cell 2. enzymes to speed up reactions Biomolecules The cells of living things are made up of 4 classes of large biomolecules LIPIDS NUCLEIC ACIDS CARBOHYDRATES PROTEINS Make up Encodes & transmits Provides a source of 1. pores/pumps for transport cell membranes genetic information energy to the cell 2. enzymes to speed up reactions acting as the border acting as the parliament of acting as Hydro Quebec of acting as bridges for transport agent of the cell the cell the cell and workers of the cell Biomolecules The major macromolecules are mostly P-O-L-Y-M-E-R-S : complex molecules made up of repeated simpler MONOMER units connected by covalent bonds. Single unit: Monomers A chain of monomers forms a P-O-L-Y-M-E-R Biomolecules e.g. starch Monosacharides Amino Acid Nucleotide Not made up of Monomer (a.k.a. simple sugars) repeating (20 different types) (5 different types) monomers (but still has an Polymer Polysacharide Peptide/Protein Nucleic Acid organization!) Biomolecules The macromolecules are composed of smaller units Most are P-O-L-Y-M-E-R-S: complex molecules made up of repeated simpler units (monomers) connected by covalent bonds. P-O-L-Y-M-E-R-S MONOMER Proteins Amino acids Nucleic acids Nucleotides Carbohydrates Monosaccharides 9 Lipids (not always a polymer) Fatty acids Biomolecules Monomer Polymer Protein Amino Acid 1 Amino Acid 2 Nucleic Acid Nucleotide 1 Nucleotide 2 Monosaccharide 1 Monosaccharide 2 Polysaccharide (disaccharide in this ca se) Metabolism Metabolism Metabolism = Catabolic and Anabolic Reactions CATABOLIC PATHWAYS ANABOLIC PATHWAYS 1. BREAK DOWN macromolecules 1. BUILD macromolecules 2. Release energy 2. Requires energy Metabolism Metabolism = Catabolic and Anabolic Reactions Food the many molecules molecules that form the cell CATABOLIC ANABOLIC PATHWAYS PATHWAYS release energy & consume energy small molecules & small molecules the many building blocks for biosynthesis  BIOMOLECULES LIPIDS NUCLEIC ACIDS CARBOHYDRATES PROTEINS Carbohydrates General Functions Energy Carbohydrates + + CO2 + O2 Water 1) source of energy and fuel for 2) storage of energy for cells 3) Building structural units in cells cells (cellular respiration) (ex: glycogen in humans) (ex: cellulose in plant cells) (ex: starch in plants) (ex: chitin in fungus & insects) Carbohydrates Monosaccharides monomers of sugars are called monosaccharides and have C, H, O for example, hexose sugars (6 carbon atoms) share the same molecular formula C6H12O6. hexose monosaccharides assume a ring configuration in solution. Glucose Galactose Fructose Carbohydrates Glycosidic Bond monosaccharides are linked together via glycosidic bonds (i.e. a type of covalent bond) formed between the carbon 1 and another carbon on an adjacent monosaccharide. glycosidic bond forms between 2 glucose monomers: Monosaccharide 1 Monosaccharide 2 Polysaccharide (disaccharide in this case) Carbohydrates Disaccharides or Intermediates When 2 monosaccharides are linked by a glycosidic bond, they form a disaccharide: 1. sucrose (glucose + fructose) 2. maltose (glucose + glucose) 18 3. lactose (galactose + glucose) Carbohydrates Polysaccharides polysaccharides are long chains of linked monosaccharides and have two primary functions: 2. 1.Energy Energystorage: storage i. Storage polysaccharide in humans called glycogen ii. Storage polysaccharides in plants are called starches 1. 2.Structural Structuralsupport: support i. Structural polysaccharide in plants is called cellulose Carbohydrates Polysaccharides Structurally they are very different! Carbohydrates Polysaccharides polysaccharides are long chains of linked monosaccharides and have two primary functions: 2. 1.Energy Energystorage: storage i. Storage polysaccharide in humans called glycogen ii. Storage polysaccharides in plants are called starches 1. 2.Structural Structuralsupport: support i. Structural polysaccharide in plants is called cellulose Carbohydrates Glycogen: energy storage in humans Energy storage when humans absorb/ingest more glucose than they can use, they store some of the excess in the form of glycogen. a glycogen polymer is heavily branched and formed of glucose monomers linked through many glycosidic bonds. Carbohydrates Glycogen: energy storage in humans Energy storage Glycogen is stored in 2 places: 1) liver cells Glycogen in liver cells (hepatocytes) regulate sugar in the entire body! When blood sugar is low: glucagon is released stimulating breakdown of glycogen into glucose in the bloodstream. Glycogen stained red in hepatocytes (liver cells) 2) Muscle cells muscle cells store glycogen but are only used for the muscle cell itself. Glycogen granules in muscle Carbohydrates Hyperglycemia STIMULUS: High levels of in bloodstream RECEPTOR: Glucose chemoreceptors CONTROL Pancreas CENTER: EFFERENT CONDUCTOR: EFFECTOR: Liver Result: decrease Hypoglycemia STIMULUS: Low levels of in bloodstream RECEPTOR: Glucose chemoreceptors CONTROL Pancreas CENTER: EFFERENT CONDUCTOR: EFFECTOR: Liver RESULT: Increase Carbohydrates Polysaccharides polysaccharides are long chains of linked monosaccharides and have two primary functions: 2. 1.Energy Energystorage: storage i. Storage polysaccharide in humans called glycogen ii. Storage polysaccharides in plants are called starches 1. 2.Structural Structuralsupport: support i. Structural polysaccharide in plants is called cellulose Carbohydrates Starch: energy storage in plants Energy storage - plants store carbohydrates in the form of starch. The starch polymer is a circular molecule found inside plant cells. Carbohydrates Polysaccharides polysaccharides are long chains of linked monosaccharides and have two primary functions: 2. 1.Energy Energystorage: storage i. Storage polysaccharide in humans called glycogen ii. Storage polysaccharides in plants are called starches 1. 2.Structural Structuralsupport: support i. Structural polysaccharide in plants is called cellulose Carbohydrates Cellulose: energy storage Structural support in plants - plants also link glucose monomers together to form long unbranched polymer chains called cellulose. The cellulose/dietary polymer is a linear molecule found in the crunchy cell wall of plant cells. Carbohydrates Amylase Amylase is an enzyme (protein) released by our salivary glands and pancreas to digest (hydrolyze) starch. Amylase can only digest starch and will not digest glycogen or cellulose. Because the starch polymer is bent, the enzymes Because the cellulose polymer is straight, the can fit into the spaces between each ring and break enzymes cannot fit into the spaces between the rings the chemical bond. such that none of the bond are broken. Amylase Cannot bind  Amylase Amylase Starch cellulose/dietary fiber Carbohydrates Digestion of Starch P-O-L-Y-M-E-R Polysaccharide Amylase Amylase INTERMEDIATE + Disaccharide Carbohydrates REVIEW  Biomolecules LIPIDS NUCLEIC ACIDS CARBOHYDRATES PROTEINS Lipids General Functions 1. Protection from cold and trauma 2. Energy reserves in the form of adipose 3. Forms the biological membranes of our cells 4. Other various functions, like hormones and cholesterol  Lipids Exception to the rule of macromolecules Unlike proteins, nucleic acids, and carbohydrates, not all lipids are made from repeating monomers. Instead of being defined by a structure, lipids are defined by a shared property: they are hydrophobic. Lipids therefore form a diverse group. Three major types of lipids: 1. Fats 2. Phospholipids 3. Steroids Lipids 1. Fats Functions of fats in biological systems Function of fats in biological systems: 1. Energy storage 2. Insulation against cold 3. Protection of internal organs 35  Lipids 1. Fats Structure: Fats = fatty acids + glycerol The long, nonpolar hydrocarbon tails of fatty acids are responsible for most of the fatty or oily characteristics of lipids. o Fatty acids are smaller units “monomers”: “Monomer” o Fats are like “polymers composed of fatty acid chains “P-O-L-Y-M-E-R-S” Example: 3 Fatty acid chains in a fat molecule Lipids 1. Fats Structure: Fats = fatty acids + glycerol - Fatty acid molecules can be linked to a glycerol molecule - A triglyceride is a lipid used for energy storage. - Number of fatty acids per glycerol can range from 1 to 3. 1 = monoglyceride 2 = diglyceride 3 = triglyceride Lipids 1. Fats Saturated Fatty Acids The carbon atoms in the hydrocarbon chain are connected to each other by single covalent bonds and are able to bind their full complement of hydrogen atoms (saturated with hydrogen). - these linear molecules can more easily stack, forming temporary interactions that stabilize them to form products that are solid at room temperature. Lipids 1. Fats Unsaturated Fatty Acids Although many of the carbon atoms in the hydrocarbon chain are linked by single bonds, some are linked by double bonds, as they DO NOT have a full complement of hydrogen atoms. - the presence of the double bond gives the molecule a “kink” preventing them from stacking well, making a product that is liquid at room temperature. Lipids 2. Phospholipids Function of phospholipids Major constituents of cell membranes. Structure of phospholipid 1 phosphate molecule 1 glycerol molecule 2 fatty acid molecules Lipids 2. Phospholipids Structure of phospholipid Phospholipids are amphipathic as they contain both hydrophilic and hydrophobic groups in the same molecule. HYDROPHILIC REGION (head) HYDROPHOBIC REGION (tails) Lipids 2. Phospholipids Function of phospholipids When placed in water, they self-assemble into a bilayer, shielding the hydrophobic portion from contacting water. 42 Lipids 3. Steroids Structure of Steroids Made from sterol: 4 fused rings Function of Steroids Cholesterol Vitamin D Constituents of cell membranes Bile Salts Hormones (produced by liver to break down fats) Lipids REVIEW LE CTURE 2 Biomolecules Proteins Nucleic Acids 101-127-AB 00001 Anatomy & Physiology for Paramedics I © Samuel Richer 2024 (adapted from Roxane Millette & Jason ) Lecture 2: Learning Objectives 1. Describe biomolecules. 2. Describe the structure and function of each class of biomolecule 1. Identification of molecules (just from chemical formula, structural formula and/or by shape) 2. Know in what food those biomolecules (nutrients) are available 3. Know in what parts of the cell/ cell organelles each biomolecule plays a role 3. Define monomer, intermediate, polymer and identify 1. carbohydrate: 1. monomer/monosaccharides: glucose/galactose, fructose, glycerol 2. intermediates/disaccharides: sucrose, maltose, lactose 3. polymers/polysaccharides: (starch, cellulose/fiber, glycogen) 2. protein: 1. monomer: amino acid, 2. intermediate : peptide/amino acid sequence 3. polymer : protein (the difference between globular proteins & fibrous proteins will be emphasized later on) 3. lipid: 1. monomer: fatty acid (saturated vs unsaturated), glycerol 2. polymer: triglyceride/fat, phospholipid, steroids. 4. Describe the functional importance of each of the biomolecules in the human body. 5. Describe which metabolic imbalances (hyperthermia and acidosis) can denature proteins and state its medical importance.  Biomolecules CARBOHYDRATES PROTEINS LIPIDS NUCLEIC ACIDS Proteins Functions So many! Amylase breaks down sugar Proteins Some other functions Proteins Enzymes drive metabolic reactions Proteins that perform functions are called Enzymes Proteins Enzymes drive metabolic reactions In the digestive system many enzymes BREAK DOWN our biomolecules POLYMER MONOMER Monosaccharides Amino Acids Fatty Acids + Glycerol Proteins Protein monomers are called amino acids Positively charged Negatively charged + Amino group Carboxyl group (NH2) (COOH) R Our proteins are made from 20 amino acids, which differ only in their R groups Proteins A chain of monomers = P-O-L-Y-M-E-R-S When amino acids are joined together they form a polymer called a POLYPEPTIDE Proteins Peptide bonds form protein polymers A P-O-L-Y-P-E-P-T-I-D-E is formed by bonding amino acids together through a peptide bond (a covalent bond specific to amino acids). ex: dipeptides are formed of two amino acids  Proteins The 4 levels of Protein Structure: Primary structure Secondary structure Tertiary structure Quaternary structure protein's unique folding and coiling of conformational shape of when more than 1 sequence of amino sections of the chain whole polypeptide chain polypeptide chain acids comes together to form the protein Proteins Primary structure Amino Primary structure: acids 1 5 10 The unique sequence of amino 15 acids in the polypeptide chain. 30 25 20 35 40 45 50 Each amino acid is connected to the next by covalent peptide 70 65 60 55 bonds. 75 80 85 90 The placement of every amino 95 acid must be accurate in order 115 110 105 100 for the protein to function correctly. 120 125 Proteins Secondary structure In addition to the primary structure (the specific amino acid sequence), proteins have additional structural characteristics which give them their unique properties. Polypeptide chains may have coiled or pleated sections A coil called an alpha helix A folded structure is called a beta pleated sheet Proteins Tertiary structure The confirmational shape (3D shape) that the whole polypeptide chain takes on. a combination of bond types determines the protein’s shape and function. Proteins Quaternary structure Sometimes more than 1 polypeptide chain come together to form a protein: Hemoglobin: Collagen: 4 polypeptides join together in this arrangement 3 coiled polypeptides join together like a rope creating to facilitate oxygen transport in blood a strong protein fiber found in connective tissue each subunit has a tertiary structure and come together to form a protein complex Proteins Primary Secondary Tertiary Quaternary Polypeptide can spontaneously organize into a complex shape PROTEIN SHAPE is essential to function Ex: receptor, antibody, enzyme  Proteins The folding of a protein is an important process! A slight change in primary structure can affect a protein’s structure & function. structure determines function Proteins Importance of the Primary Structure Proteins Protein Denaturation: PROTEINS are FRAGILE If they lose their 3D structure (unravel) they become non-functional (denatured). Heat (thermoregulation), salt (natremia & kalemia), acidity (acidosis, alkalosis) can all cause denaturation of proteins Protein REVIEW  Biomolecules NUCLEIC ACIDS CARBOHYDRATES PROTEINS LIPIDS Structure Nucleic Acids Monomers & Polymers Monomer Polymer Nucleotide Nucleic Acid A T Nucleic Acids Monomers & Polymers Polymers made up of many nucleotide monomers bonded together in a long chain Monomer Polymer Nucleic Acid FOUR KINDS: TWO KINDS: In DNA In RNA DNA Deoxyribonucleic Acid ✓ Thymine ✓ Uracile RNA Ribonucleic Acid ✓ Guanine ✓ Guanine ✓ Adenosine ✓ Adenosine ✓ Cytosine ✓ Cytosine Nucleic Acids Nucleotide = Monomer A Phosphate Nitrogenous Sugar base Each nucleotide has 3 components Nucleic Acids Nucleotide = Monomer A Phosphate Nitrogenous Sugar base Deoxyibose Ribose sugar is found in sugar is found DNA in RNA Nucleic Acids Nucleotide = Monomer A Phosphate Nitrogenous Sugar base Nitrogenous Bases found in RNA Nitrogenous Bases found in DNA Uracil (U) Nucleic Acids DNA vs. RNA Structure DNA is RNA is double stranded single stranded - It has 2 long strands - It has 1 long linked together by polynucleotide strand hydrogen bonds that twists around itself between their nitrogenous bases. -Looks like a twisted ladder Nucleic Acids In DNA In RNA Phosphate Sugar Deoxyribose Ribose Adenine (A) Adenine (A) Guanine (G) Guanine (G) Bases Cytosine (C) Cytosine (C) Thymine (T) Uracil (U) Double stranded DNA Single stranded RNA Nucleic Acids Complementarity of DNA The sugar-phosphate backbones of the strands wrap like a ribbon around the outside of the double helix. The bases pairs point inwards and stabilize the structure through H-bonds. Nucleic Acids Complementarity of DNA The two strands of DNA are not identical, but complementary: - This occurs as the nitrogenous bases pair with each other via hydrogen bonds. This allows for the formation of the double helix. A binds with T C binds with G Function of DNA & RNA Nucleic Acids DNA Functions 1. Makes up our genes, the instructions for making proteins, essential to the cell’s life 2. Transmit genes to offspring: Making a sperm and an egg Nucleic Acids RNA Functions RNA is used as a messenger: it transports an RNA copy of the DNA instructions out of the nucleus and into the cytoplasm to build a protein.  Nucleic Acids DNA v.s. RNA DNA and RNA are polymers composed of nucleotides and differ in structure and function. DNA is commonly found in the RNA has many more functions nucleus of a cell and stores an inside the cell, including acting organism’s genetic information. as blueprints for proteins. It is It is most commonly found as a most commonly found as a double strand. single strand. Nucleic Acids Nucleic Acid Functions Proteins need to be made all the time by cells How do the instructions for making a protein (DNA in nucleus) get converted into a protein? Each gene on a DNA has a unique nucleotide sequence that codes for the building of a particular amino acid sequence. This process includes 2 steps 1. making a copy of the instructions DNA → mRNA (in the nucleus) 2. making protein from instructions mRNA → PROTEINS (in cytosol)  DNA 1 Synthesis of mRNA in the nucleus mRNA NUCLEUS CYTOPLASM 1. In order to make a protein, a copy of the nucleotide sequence (length of the gene) must be made. The copy is a messenger RNA strand (mRNA)  DNA mRNA NUCLEUS CYTOPLASM mRNA 2 Movement of mRNA into cytoplasm via nuclear pore 2. The mRNA copy leaves the nucleus and enters the cytoplasm  DNA mRNA NUCLEUS CYTOPLASM 3. The nucleotide sequence of the mRNA strand is then translated with the help of a ribosome into Ribosome an amino acid sequence of the desired protein mRNA 3 Synthesis of protein Amino Polypeptide acids Nucleic Acids Deoxyribonucleic Acid (DNA) DNA language is translated into a protein language, forming the primary structure of a protein (linear arrangement of the amino acids). This 1 o structure then determines the 2 o and 3o structures of the protein. 40 Function of ATP Nucleic Acids Nucleotides can also act as sources of energy A cell’s primary source of energy comes from ATP, or adenosine triphosphate. NITROGENOUS BASE SUGAR Phosphate The arrangement of the molecule is very similar to the nucleotide in RNA with simply 2 additional phosphate groups. Nucleic Acids Energy storage - Cells store energy in the covalent bond between the 2nd and 3rd phosphate groups of ATP. - These bonds are said to be high-energy because the resulting phosphate group is very reactive once broken from ATP Nucleic Acids Energy storage - The addition of a phosphate group (called phosphorylation) to proteins, like certain enzymes or pumps, can “activate” them. - Breaking ATP turns into ADP.  substance conducts electricity does not conduct electricity ionic (charged) electrons are transferred covalent molecule Na+, K+ (function as signal) electrons are shared mix with water (hydrophilic) does not mix with water (hydrophobic) slightly charged Uncharged, covalent non-polar covalent polar lipids (function to compartmentalise fluid environments) carbohydrates proteins (function as fuel source) (function to build structures)  Glucose Preferred fuel for cell resp cellulose fiber carbs starch not humans present in plants monomer polymer glycogen: short term storage of fuel for energy production amino acid: last resort fuel for cell respiration monomer proteins (hormones, enzymes, carrier proteins) polymer BIOMOLE CULES fatty acid & glycerol fuel for cell resp monomer fat: long term storage of fuel for energy production lipids phospholipid: structural: membrane polymer steroid: functional globular hormones LE CTURE 4 Digestive System 101-127-AB 00001 Anatomy & Physiology for Paramedics I © Samuel Richer 2024 (adapted from Roxane Millette)  Substance conducts electricity does not conduct electricity ionic (charged) electrons are transferred covalent molecules Na+, K+ (function as signal) electrons are shared mixes with water (hydrophilic) does not mix with water (hydrophobic) slightly charged Uncharged, covalent non-polar covalent polar lipids (function to compartmentalise fluid environments) carbohydrates proteins (function as fuel source) (function to build structures)  Biomolecules Carbs Proteins Lipids mono mono mono saccharides amino acid fatty acid glucose galactose fructose di peptide di poly poly saccharides saccharides protein glycerol maltose poly lactose sucrose Cellulose starch glycogen Dietary Fiber triglyceride diglyceride/ steroid/ fat phospholipid cholesterol Glucose Preferred fuel for cell resp cellulose fiber Carbs starch not humans present in plants monomer polymer Glycogen: short term storage of fuel for energy production Amino Acid: last resort fuel for cell respiration monomer Polypeptide / Protein Proteins hormones, enzymes, carrier proteins polymer Biomolecules Fatty Acid & Glycerol fuel for cellular respiration monomer Fat: long term storage of fuel for energy production Lipids Phospholipid: structural: membrane polymer Steroid: functional globular hormones  Cellular Respiration ATP From Digestive System All cells need energy! Carbohydrates + + CO2 From Respiratory System Removed by Respiratory System Oxygen O2 + Water Excreted in Urinary System Anatomy of the Digestive System Function of the Digestive System 1. Move food through the digestive tract 2. Secrete gastrointestinal juices and food digestion 3. Absorb nutrients, water & electrolytes 4. Circulate blood through the gastrointestinal organs to carry away absorbed substances to all the cells of the body Inputs & Outputs of the Digestive System Absorption The movement of nutrients, salts & water into the Gastrointestinal Tract Digestion The breakdown of food components Types of Digestion Mechanical/Physical Chemical Digestion Digestion Types of Digestion Food is broken down in two ways along the gastrointestinal tract (GI tract) Mechanical/Physical Chemical Digestion Digestion Change that does NOT Change that makes a new result in a new substance substance Types of Digestion Mechanical/Physical Digestion Change that does NOT result in a new substance Types of Digestion Chemical Digestion Change that makes a new Chemical digestion occurs using substance proteins called ENZYMES! Types of Digestion CHEMICAL DIGESTION by Enzymes In the digestive system many enzymes BREAK DOWN our biomolecules POLYMER MONOMER Monosaccharides Amino Acids Fatty Acids + Glycerol Journey through the Gastrointestinal Tract 1. Mouth, Teeth, Tongue, Salivary Glands Function: ❑ Break up food ❑ Digest starch ❑ Kill germs ❑ Moisten food 1. Mouth, Teeth, Tongue, Salivary Glands Mechanical/Physical Digestion o Teeth masticate and breaking up the food Chemical Digestion o Saliva secreted by the salivary glands. Composed of: 1) Amylase initiates the digestion of starch (carb) Amylase + 2) Mucus serves as lubricant 3) Electrolyte solution (Na+, Cl-, K+, HCO3-) moistens food 4) Anti-bacterial chemicals Kills bacteria that enters mouth 1. Mouth, Teeth, Tongue, Salivary Glands Amylase enzyme in saliva starts to break down starch The salivary glands Starch Salivary Amylase Disaccharides 2. Epiglottis Function: ❑ Epiglottis blocks the passage to respiratory system ❑ Epiglottis directs food to esophagus 2. Epiglottis  Case Study An elderly man, is eating a Big Mac after a bad day. While laughing mid-bite, he suddenly starts coughing and appears to be struggling to breathe. His friends notice that he’s not able to speak clearly, and his face is turning red. He’s gripping his throat with one hand, indicating distress. By the time paramedics arrive, he’s showing respiratory distress, including difficulty breathing, a muffled voice, and drooling. As paramedics, you approach the patient and conduct an initial assessment. 1. What might have prevented the epiglottis from protecting his airway? 2. As paramedics, what steps should you take immediately to assess and address his airway obstruction? 3. If conventional methods don’t work, what alternative procedures should you consider? 4. Describe the role of the epiglottis during any advanced airway procedures you might need to perform 3. Esophagus Function: ❑ Muscular tube which food is passed on from the pharynx to the stomach 3. Esophagus The muscular esophagus carries food from the pharynx to the stomach PERISTALSIS: Series of involuntary wave like muscle contractions which move food along the digestive tract 4. Stomach Function: Sac-like expansion of the GI tract ❑ Kills germs ❑ Break up food ❑ Digest proteins ❑ Store food 4. Stomach Food is temporarily stored here (can stretch to fit 2L!) Chemical Digestion: Mechanical/Physical Digestion: Gastric juices secreted to break down food Layers of muscle contract to break down food Gastric Juice Muscular contraction (Peristalsis) Stomach 4. Stomach Chemical Digestion: Stomach cells secrete Gastric juices = 3D folded mature protein Hydrochloric Acid (HCl) Hydrochloric + Acid (HCl) Pepsin denatured protein Pepsin short peptide chains 4. Stomach Mechanical Digestion Layers of muscle line the inside wall to break down food 1. Inner oblique muscle layer 2. Middle circular muscle layer 3. Outer longitudinal muscle layer 4. Stomach Two involuntary sphincters keep the high acidity pH from HCl in the stomach  Case Study As you get older, the muscle of the lower esophageal sphincter gets weaker and weaker. The contractions of this muscle become not as great. 1. What may a patient suffer from due to this physiological change 2. Why does this usually happen in the morning when you wake up? 3. What might be prescribed to alleviate this 5. Accessory Organs Liver Function: ❑ Produces bile which is released in the small intestine to breaks up fat Gallbladder Function: ❑ Pouch structure near liver that concentrates & stores Bile Pancreas Function: ❑ Releases digestive enzymes in intestine ❑ proteases to digest proteins ❑ amylases to digest starch ❑ Releases hormones ❑ Glucagon ❑ Insulin  5. Accessory Organs Liver Gallbladder Bile Bile o Is made in the Liver o Excess is stored in the Gallbladder o Bile Is secreted into the small intestine o Emulsifies large fat drops into triglycerides Bile  5. Accessory Organs PANCREASE Peptidases Amylase Lipases An organ which secretes both: 1. Hormones (endocrine) 2. Digestive enzymes (exocrine) →Glucagon → Peptidases →Insulin → Amylases → Lipases Chemical Digestion: (in the small intestine) Pancreatic Peptidases are secreted into the small intestine peptidases dipeptides short peptide chains Pancreatic Amylases are secreted into the small intestine Polysaccharides Amylase Disaccharides Lipases are secreted into the small intestine Triglycerides Lipases 3 fatty acids + glycerol 6. Small Intestine Function: Long, narrow, coiled tube extended from the stomach PART 1: DIGESTION ❑ Most chemical digestion occurs here PART 2: ABSORBTION ❑ Monosaccharides and amino acids are absorbed into the inner lining ❑ Fatty Acids and glycerol go to the lymphatic system  6. Small Intestine 3 Regions of the small intestine Duodenum = mostly digestion Jejunum = absorption of nutrients Ileum = absorption of nutrients and water 6. Small Intestine The Villus and Microvilli increases surface area of absorption GREATLY  6. Small Intestine Lactase Maltase Recombine Sucrase 3 fatty acids + glycerol Triglyceride Disaccharide LIPID ABSORBPTION 1. The fatty acid and glycerol CARBOHYDRATE monomers are reassembled into polymers inside the intestinal cell. ABSORBPTION 1. Lactase, maltase and 2. The resulting lipid is absorbed sucrase enzymes on the into lymphatic capillaries. border of the cells of the small Amino intestine digest disaccharides Acid into monoscaccharides. 2. Monosaccharides absorbed by diffusion into the Dipeptide vein of the blood strea