Anatomy PDF Study Notes

 Explain all lectures  Explain all labs  MCQ questions  OSPE questions  Anatomy Anatomical positions ➋ Human body is ➊ standing erect...

 Explain all lectures  Explain all labs  MCQ questions  OSPE questions  Anatomy Anatomical positions ➋ Human body is ➊ standing erect ➌ ➋ eye looking forward ➍ ➌ upper limb by side ➍ palm directed forward ➎ lower limb close together ➎  Supine position :- body lies on back face directed upwards  Prone position :- body lies on face face is directed downwards  Lateral position :- body lies on one side  Lithotomy position :- Person lies supine with hips and knees semiflexed, thighs abducted and feet strapped in position. Supine Prone Lateral Lithotomy position Anatomical plane  Median plane “mid-sagittal” :- vertical plane divides body into equal Rt. & Lt. halves  Para-median plane “para-sagittal”:- vertical plane passes parallel to sagittal or median plane divides body into unequal Rt. & Lt. halves  Coronal plane “frontal” :- vertical plane divides body into anterior & posterior parts  Horizontal plane “Transverse” :- Transverse plane divides body into upper & lower parts  Anatomy  According to the shape of bones :-  Long bones o Length greater than width o Composed of two ends (epiphyses) and a shaft (diaphysis) o e.g. femur, radius, ulna , humerus  short bones o Cube shaped o e.g. carpal, tarsal bones  Flat bones o Thin, flattened, a bit curve o e.g. ribs, sternum, skull bones, scapula  Irregular bones o e.g. verterbrae , facial bones, hip bone.  Anatomy Joint  Definition :- Meeting two or more bones of skeleton  Function :- Hold skeleton together & Allow for mobility and flexibility of skeleton  Classification :- Structure Function (Based on nature of tissue (Based on degree of motion ) between articulation bone) Synarthrosis Fibrous “Nonmovable” Amphiarthrosis Cartilaginous “Slightly movable” Diarthrosis Synovial “Freely movable” Fibrous joints  Characters :- 1. The opposed bony surface are connected together by fibrous tissue 2. No joint cavity between articulating bones 3. No movement is allowed between articulating bones  Types :- 1. Sutures fibrous joints  These joints ossify with age  Occurs between flat bone e.g. skull bone  Anatomy Muscle  Type :- Skeletal muscle Smooth muscle Cardiac muscle Distribution Attached to skeleton In wall of viscera and In wall of heart blood vessels (myocardium) Microscopic Muscle fibers are Muscle fibers are Muscle fibers are appearance multinucleated & show spindle shaped , uninucleated & show transverse striations uninucleated & show no transverse striations & striations branched Nerve supply Somatic motor nerve Autonomic Autonomic Control Voluntary Involuntary Involuntary Function -produce different Control swallowing , Responsible for its movements of body urination , defecation rhythmic contraction -contractions pump venous blood to heart -heat production of body -Maintain posture and body position Skeletal muscle  Skeletal muscle is formed of muscle fibers each fiber surrounded by sheath “Endomysium” Structure  Muscle fibers are arranged in bundle “fascicles” surrounded by “Perimysium”  Whole muscle is surrounded by strong sheath “Epimysium”  Anatomy Nervous system Nervous system Central nervous Peripheral nervous system system Somatic nervous Autonomic nervous Brain Spinal cord system system Cranial nerve Cerebrum Cerebellum Brain stem. Sympathetic Spinal nerve Mid brain Parasympathetic Medulla Cerebrum Pons Cerebellum Mid brain Pons Cerebrum Medulla  Largest part of the brain. It occupies anterior & middle cranial fossae.  It is divided into right and left cerebral hemispheres by median longitudinal fissure.  Each hemisphere has three surfaces  supero-lateral , medial , inferior Median longitudinal fissure Medial surface Median longitudinal fissure Lt. hemisphere Rt. hemisphere Inferior surface Grey matter White matter Lateral Ventricle Basal  Anatomy “Motor cortex” “Sensory cortex” “Visual cortex” “Auditory cortex” Cerebellum  It occupies posterior cranial fossae.  Has two surfaces  upper & lower and 3 lobe  Ant. & Middle & Post. - Provides pathway of tracts between cerebral cortex & spinal cord Brain stem - Origin of nuclei of cranial nerves (from Cr3 to Cr12) 1. Medulla oblongata :-  Lowest part of brain stem Midbrain  Extent :- above  pons below  spinal cord  Giving exit to 9th , 10th , 11th , 12th cranial nerve 2. Pons :- pons  Extent :- above midbrain below  medulla th th th th  Giving exit to 5 , 6 , 7 , 8 cranial nerve 3. Midbrain :- Medulla  Extent :- above cerebrum below pons  Anatomy THE SKULL  The skull is the skeleton of head  Structure :- formed of 22 bone  One movable bone  Mandible which articulate by synovial joint  21 immovable bone articulating together by fibrous joint Parts of skull 8 paired bone (Rt.&Lt.) 5 unpaired bone 1. Cranium  upper , post. Part which Parietal encloses brain Frontal Temporal 2. Facial  ant. Part of skull Ethmoid Zygomatic Sphenoid Lacrimal Occipital Maxillary Vomer Nasal Palatine Inferior chocha THE NORMA VERTICALIS “Vault” A. Bone forming it  4 bones 1. Frontal bone :- anteriorly 2. 2 parietal bone :- on each side 3. Occipital bone :- posteriorly B. Sutures between bone  1. Coronal suture :- runs transversely between frontal bone & 2 parietal bone 2. Sagittal suture :- runs in median plane , connecting 2 parietal bone 3. Lambdoid suture :- runs between occipital bone & 2 parietal bone C. Special features  1. Bregma :- point of meeting between sagittal & coronal suture. at birth this area is occupied by rhomboidal shaped membrane called Ant. Fontanelle which ossifies at age 18 months 2. Vertex :- is middle of sagittal suture & highest point of skull 3. Lambda :- point of meeting between sagittal & lambdoid sutures. at birth this area is occupied by triangular membrane called Post. Fontanelle which ossifies at age 6 months  Anatomy THE NORMA LATERALIS A. Bone forming it  1. Parietal bone 2. Frontal bone 3. Occipital bone 4. Greater wing of sphenoid bone 5. Squamous , mastoid parts of temporal 6. Zygomatic bone 7. Maxillary bone 8. Lacrimal bone 9. Nasal bones B. Special features  1 1. Temporal line :- start anteriorly at zygomatic process of frontal bone. it divides into 4  Superior Temporal line :- gives attachment to temporal fascia 2 5 3  Inferior Temporal line :- gives origin to temporalis muscle 2. Supramastoid crest :- passes above mastoid process to reach post. end zygomatic process of temporal bone  Anatomy 3. Zygomatic arch :-  bony bridge formed of temporal process zygomatic bone “Ant.” & zygomatic process of temporal bone “Post.”  lower border gives origin to masseter muscle 4. Pterion :-  Area of meeting of 4 bones [ frontal , parietal , squamous temporal , greater wing of sphenoid] connected by H shaped suture  At birth , pterion is occupied by membrane called antero-lateral “Sphenoidal” fontanelle which ossifies at age of 3 months  Centre of pterion is related to ant. branch of middle meningeal artery 5. Asterion :-  Area of meeting of 3 bones [ parietal , mastoid temporal , occipital]  At birth , Asterion is occupied by membrane called postero-lateral “Mastoid” fontanelle which ossifies at age of 3 months 6. Temporal fossa :-  Boundaries :-  Sup. temporal line :- above & behind  Zygomatic arch :- below  Frontal process of zygomatic bone :- anteriorly 6  Gives attached to temporalis & masseter muscle 7. Infra-temporal fossa :- 8 9  Boundaries :- 10 7  Post. surface of maxilla :- Anteriorly ⓵  Lateral pterygoid plate :- medially ⓶  Ramus of mandible :- laterally  Styloid & temporal process :- posteriorly ⓷ 11  Communication :-  Orbit through inf. Orbital fissure  Temporal fossa through gap deep to zygomatic arch  Pterygopalatine fossa through pterygomaxillary 2 1 3 fissure  Content :-  2 muscle  med. & lat. Pterygoid muscle  2 vessels  maxillary artery & vein  3 nerve  mandibular & maxillary nerve & chorda tympani 8. External auditory meatus :- Mandibular fossa Tympanic plate External auditory meatus Mastoid process Articular tubercle Styloid process  Histology Cell  Definition :- Basic structural & functional unit of the living body  Functions :- absorption , respiration , secretion , excretion , sensation , conduction , contraction , movement , reproduction.  Size :- Varies  Shape :- Rounded , oval , flat , stellate , polygonal , cubical , columnar.  Structure:- Animal cell is eukaryotic formed of two basic components :  Cytoplasm  Nucleus Cytoplasm It is formed of :  Cytosol :- Fluid containing “Carbohydrates , proteins , lipids , Minerals. , Ions and salts , 02 and CO2  Organelles  Inclusions. Cytoplasmic organelles Classified according to presence of limiting membranes into: Membranous organelles Non Membranous organelles  Covered by membrane  Uncovered by membrane  Contain enzymes  No enzymes 1. Plasma membrane 1. Ribosomes 2. Mitochondria 2. Cytoskeleton 3. Endoplasmic reticulum 3. Microtubules 4. Golgi apparatus  Centrioles 5. Lysosomes  Cilia 6. Peroxisomes  Flagella 7. Endosomes 4. Filaments 8. Coated vesicle 5. Proteasomes. Cell membrane = plasma membrane = plasmalemma  Definition :- limiting membrane that envelopes all the cells.  By LM :- Difficult to be seen because it is very thin (7.5-10 nm). Can be demonstrated when stained with silver (Ag)or PAS stains.  BY EM :- Two electron-dense (dark) layers separated by an intermediate electron-  Histology lucent (light) layer. Thus it is called trilaminar membrane or unit membrane. There is a fuzzy material found on the outer surface only, which represents the cell coat “glycocalyx” Trilaminar (3 layer) Cell coat Outer dark Middle light Inner dark  Molecular structure of cell membrane 1. Lipid : consists of phospholipids and cholesterol.  Phospholipid molecules:- arranged into 2 layers (lipid bilayer). Each molecule has: Head Tail  Is charged.  Is non-charge d  Polar  Non polar,  Hydrophilic.  Hydrophobic  Cholesterol molecules :- among the hydrophobic fatty acids Functions :  Restricting movement of phospholipid molecules so stabilize the membrane  Modulating fluidity of membrane preventing it from being tm fluid or too rigid 2. Protein :- about 50% of total membrane mass, present in two forms: A. Peripheral proteins B. Integral proteins (transmembrane proteins) :- Embedded in lipid bilayer.  Two types are present: Channel proteins for transport of ions and water Carrier proteins for transport of small polar molecules as glucose and ions as Na K pump, 3. Carbohydrates :- at external surface formed of: A. Glycoproteins : oligosaccharide chains linked to protein molecules. B. Glycolipids : oligosaccharides linked to phospholipid molecules.  Cell coat (glycocalyx) :- Formed of molecules of glycoproteins & glycolipids Functions :- Cell adhesion , Cell identification , Cell protection , Cell immunity , Receptor functions.  Histology  Inner nuclear membrane :- It is fibrillar due to attached chromatin threads (peripheral chromatin). It is associated with nuclear lamina formed mainly of Lamins for stabilization of nuclear envelope  Nuclear pore complex :- formed of 8 protein subunit “each subunit formed of 3 parts” & central channel  Function :-Transport of proteins to the nucleus & export of RNA & ribosomal subunits to the cytoplasm through transporter protein. Chromatin  Definition :- In non-dividing nuclei chromatin is chromosomal material in uncoiled state. It represents genetic material, formed of nucleoproteins (Double-stranded DNA + Histones &non histone protein ). found in two forms: Euchromatin Heterochromatin It is coiled inactive chromatin It is extended (uncoiled) chromatin Contains inactive genes Contains active genes Predominates in metabolically inactive cells e.g. Predominates in metabolically active cells Lymphocytes as in protein forming cells e.g. nerve cell & L.M : coarse clumps corresponding to dark liver cell L.M : fine threads corresponding to pale basophilic nucleus with un-clear nucleolus basophilic nucleus with clear nucleolus E.M: It appears as electron dense E.M: It appears as electron lucent Sites of heterochromatin :-  Peripheral chromatin: attached to the inner surface of nuclear membrane.  Chromatin islands: aggregated clumps scattered in the nuclear sap.  Nucleolus-associated chromatin: condensed around the nucleolus  Histology Simple squamous epithelium.  Formed of ONE layer of flat cells with flat nuclei resting on basement membrane.  Functions :- It provides  smooth surface which is important for easy passage of fluids and easy movement.  A thin membrane that helps exchange of gases.  Sites :-  Lines blood vessels & heart forming smooth surface and is called endothelium  Lines lung alveoli thin membrane for exchange of gases and called pneumocytes.  Lines serous membranes e.g. pleura, pericardium & peritoneum called mesothelium  Lines Bowman's capsule of kidney (filtration of blood). Simple cubical epithelium.  Formed of ONE layer of cube-like cells with central rounded nuclei.  Functions :- Secretion and reabsorption.  Sites :-  Acini & small ducts of all exocrine glands. e.g. salivary glands.  Thyroid follicles.  Convoluted tubules of kidney Simple columnar epithelium.  Formed of ONE layer of tall columnar cells with basal oval nuclei  Function :- Secretion and absorption.  Sites :-  Lines stomach (secretion).  Histology Collagen fibers Elastic fibers Reticular fibers Elastin and microfibrils of Structure Type I collage Type III collage fibrillin - Wavy branching bundles By LM. - Single, thin and branching irregular branching and formed of non-branching fibers -White glistening in fresh - Yellow in fresh sections anastomosing forming sections network Staining Eosin → Pink Eosin → Pink Eosin → Not visible Mallory’s trichrome → Blue Orcein → Brown Silver → Brown black Van Gieson → + Red Van Gieson → +yellow PAS → MagentaRed - Strong, resist - Loose flexible Character stretching - Stretch and recoil= elastic supporting network - Flexible but inelastic - Resist boiling - Boiling-> Gelatin - Give elasticity - Form a flexible - Give strength and Function network in the stroma resist stretching of organs as spleen, lymph nodes, liver and endocrine lands  Types of collagen :- 20 types but the most common MCQ !!!  Type I collagen “most common” :- Found in dermis , tendons, ligaments, fascia, bone, fibrocartilage, dentin, capsules of organs, and sclera.  Type II collagen :- Found in hyaline cartilage and vitreous body of the eye.  Type III collagen “reticular fibers” :- Found in liver, spleen, lymph node.  Type IV collagen :- Associated with basal laminae (Basement membrane).  Collagen synthesis :- Prepro-collagen chain of amino acids:- Pro-collagen Tropo-collagen Collagen fibril Collagen fiber Glycine, Lysine, Proline, Triple helix Hydroxyproline, Hydroxylysine Fixed Transient CT. cells Fibroblasts Plasma cells Pigment cells Lymphocytes Adipocytes Neutrophils Pericytes Eosinophils Mast cells Basophils Macrophages Monocytes Macrophages  Physiology Homeostasis of Blood pressure Pressure  Baroreceptors in walls of blood vessels detect an increase in BP  Brain receives input and signals from BV. and heart  Blood vessels dilate, HR decreases  BP decreases ↑ blood pressure = response Lying down ↑ heart rate = effector -ve feedback Standing up BP receptor stimulation = sensor ↓ blood pressure = stimulus +ve Feedback Mechanism  A mechanism that brings greater change in the same direction.  The effect of regulating system magnifies the error and sets in vicious cycle (an effect stimulates itself) which stops only when the initial stimulus is removed.  Example of +ve feedback Blood loss 1.Oxytocin secretion during parturition Ineffective heart pump 2. Enzymatic cascade for blood coagulation ↓B.P. 3. Lactation ↓blood flow to heart muscle Weakness of heart muscle ↓heart pump  Physiology Thermoregulatory Mechanism on exposure to cold Mechanism of increasing heat production 1. Increased muscle tone & shivering 2. Increased secretion of thermogenic hormones as Catecholamine & Thyroxin Mechanism of decreasing heat loss 1. Cutaneous Vasoconstriction 2. Radiation and Conduction Thermoregulatory Mechanism on exposure to heat Mechanism of increasing heat production 1. Decreased muscle tone 2. Decreased secretion of thermogenic hormones Mechanism of decreasing heat loss 1. Cutaneous Vasodilatation 2. Sweat secretion Hormones in heat stress 1. Antidiuretic hormone (ADH) is released to increase water reabsorption from kidneys. 2. Aldosterone is released to increase the reabsorption of sodium. Fever “Raised central temperature” Hyperthermia Pyrexia  Elevation of body temperature above set point due to disturbance of temperature regulating center.  Important sign of something going wrong in body & It is part of body’s response to disease.  Causes :-  Infection :- due to bacteria, viruses and protozoa.  Tissue destruction:- e.g. cardiac infarction, uninfected neoplasm and rheumatic fever.  Abnormalities in brain itself.  Brain tumors.  Dehydration.  Pyrogens :- group of substance that cause set point of hypothalamic thermostat to rise “FEVER” e.g.  Lipo-polysacharide  Physiology Water balance Water gain “Input” = Water loss “Output”  Water gain “input” 2600 ml/day  Exogenous water “main source” about 2250 ml/day , and it includes :-  Water that are drunk , about 1500 ml/day  Water present in eating food , about 750 ml/day  Endogenous water “metabolic by oxidation of H2” , about 350 ml/day  Water loss “output” 2600 ml/day  1500 ml in urine  100 ml in feces  400 ml by evaporation from respiratory tract  600 ml from skin Control of Water balance  Water intake & water loss are controlled by plasma osmolality which depends on its Na+ concentration  Increase plasma osmolality lead to increase water intake & decrease water loss.  Decrease plasma osmolality lead to decrease water intake & increase water loss.  Water intake is controlled by thirst  water loss is controlled by ADH. ADH ADH Diuresis Anti-diuresis Hypo-osmolality Set point Hyper-osmolality ↓ Water intake ↑ water intake Thirst Thirst  Hyper-osmolality in cases Dehydration  Physiology  Gated channels → They have gates that open or close.  Voltage gated :- open or close by alterations in membrane potential (i.e., in neurons and muscle cells)  Ligand gated :- Open or close by binding to a ligand (i.e., acetylcholine (A.Ch.) channels in nerve cells)  Mechanically-gated :- (i.e., cilia-like projections on hair cells of inner ear).  Water channels :- formed of groups of membrane proteins called aquaporins. Ligand Factors affecting rate of diffusion 1. Permeability of the membrane : Increased permeability increase diffusion rate , is influenced by following factors :  Temperature :- Increased temperature increase diffusion rate  Lipid solubility of substance :- Increased lipid solubility increase diffusion rate.(oil/water partition coefficient)  Molecular weight of diffusing substances :- Increased M.W decreases diffusion rate.  Thickness of the membrane:- Increase thickness decrease diffusion rate.  Number of protein channels:- Increased number of protein channels in unit area increase rate of diffusion. 2. Surface area of membrane : Larger surface area of membrane increase diffusion rate 3. Concentration difference (= concentration or chemical gradient) 4. Electrical potential Fick's law of diffusion Diffusion rate (J) = ∆ CX A X KP Concentration gradient (C) X surface area (A) X permeability coefficient (Kp) KP : permeability coefficient is an index for rate of movement of a substance across membrane.  Biochemistry Photosynthesis ―Anabolism‖ Light 6CO2 + 6H20 C6H12O6 + 6O2 Carbon dioxide Water Glucose Oxygen Cellular respiration ―Catabolism‖ C6H12O6 + 6O2 6CO2 + 6H20 + ATP Glucose Oxygen Carbon dioxide Water Energy ATP (Energy Currency)  Components :-  Adenine → Nitrogenous base  Ribose → Five-carbon sugar  Phosphate group → Three phosphate group  Three phosphate groups (two with high energy bonds.)  Second and last phosphate group contain the MOST energy.  Levels for sources for ATP synthesis  Cellular respiration (oxidative phosphorylation)  in presence of oxygen for example (aerobic glycolysis ).  Anaerobic conditions (substrate-level phosphorylation)  in absence of oxygen for example (anaerobic glycolysis).  Biochemistry + H3N - Val Cys coo Leu Pro N-terminal C-terminal 2. Secondary structure :-  Definition :- coiling and folding of the polypeptide chain  Bonds responsible:- Hydrogen bond. It is the bond between hydrogen of -NH group of one amino acid residues and the carbonyl oxygen (C=O) of fourth one  Mechanism :- interaction of adjacent amino acid residues (first and fourth).  2 main forms :- -helix ―most common‖ β-pleated sheets Shape & formation : It is a rod like Shape & formation : structure with peptide bonds coiled  This structure is formed between two or more separate tightly inside and side chains of residues polypeptide chains. It may also be formed between (R) extending outward from chain. segments of same polypeptide chain. Characteristics:  Hydrogen bond is also responsible for its formation. It 1) Each (C=O) of one amino acid is occurs between (-NH) group of one chain (or segment) hydrogen bonded to the (-NH) of next and (C=O) of group of adjacent chain (or segment). fourth amino acid in chain (1→4 ) Two types of β-sheets are present: 2) Complete turn distance equals 54 nm. 1) Parallel β-sheets :- in which two polypeptide chains run 3) Each turn contains 3.6 amino acids in & same direction. residues. 2) Antiparallel β-sheets: in which two polypeptide chains run in & opposite direction.  Biochemistry Enzymes  Definition :-These are specific protein catalysts that accelerate rate of chemical reactions Enzyme Substrates Products Substrates :- substance upon which the enzyme acts ―binds a specific site on enzyme and undergoes a chemical transformation‖ Active site : - region of an enzyme surface to which a substrate binds. Allosteric site :- Site that allows another molecule to either activate or inhibit enzyme activity  properties :-  They are protein in nature , Exceptions include Ribozymes (RNA) which catalyze splicing of RNA.  Not affect equilibrium constant (i.e. end products) of reactions  They act within a moderate pH and temperature range.  Enhance rates by factors of 106 to 1012  Synthesized in cell but can act either intra or extracellular Intracellular enzymes: Produced and act inside cells e.g. metabolic enzymes. Extracellular enzymes: Produced inside cells and act outside cells e.g. digestive enzymes.  They are highly specific. catalyzing only one type of chemical reaction. There are 4 types of specificity 1. Absolute specificity: one enzyme acts only on one substrate e.g. glucose oxidase act on glucose only 2. Relative specificity : one enzyme acts on a group of substrate  Bond specificity : e.g. proteolytic enzymes act on peptide bonds & lipases act on ester bond.  Biochemistry Enzyme inhibitor Reversible inhibitors Irreversible inhibitors Bind to enzymes through non covalent bonds. - Dilution of the enzyme-inhibitor complex dissociates the reversibly bound inhibitor and recovery of enzyme activity. Non-Competitive inhibitors Competitive inhibitors  Similar to substrate.  Inhibitor and substrate bind to  This type of inhibition cannot be  compete with substrate for active site of different sites on enzyme. reversed by adding more substrate the enzyme.  The inhibitor does not alter the  The inhibitor alters the  Both substrate (S) and inhibitor (I) can catalytic site. catalytic site. bind with catalytic site of enzyme to form  There is no structural similarity  Irreversible inhibitors include either Enz-S-complex or Enz-l-complex. between substrate and inhibitor. the following:  Combination between enzyme and substrate  The inhibitor can bind either free or inhibitor depends on: enzyme or the enzyme-substrate 1. Cyanide and carbon - Concentration of substrate. complex. Both enzyme inhibitor monoxide inhibit cytochrome oxidase - Concentration of inhibitor. complex and enzyme substrate - Affinity of both inhibitor and inhibitor complex are inactive. substrate to active site of the  Effect of noncompetitive inhibitor enzyme. on Vmax and K: 1) Vmax is decreased.  Example of competitive inhibitors:- 2) Km is unchanged. Malonate and Succinate: both compete for catalytic site of Succinate DH.  Effect of competitive inhibitor on Vmax and Km: 1) Effect on Vmax: not affect Vmax. 2) Effect on Km: increases Km Zymogens They are inactive enzymes. 1. Zymogens are inactive because their catalytic sites are masked by a polypeptide chain. 2. 2. Activation of zymogen, into active enzyme is done by removal of the polypeptide chain to open the catalytic site for its substrate. 3. 3. Examples of zymogens: are pepsinogen and trypsinogen.  Biochemistry  Store energy in form of :-  starch (in plants)  glycogen (in animals and humans)  Supply carbon for synthesis of other compounds  Important structural components in animal and plant cells.  Important part of nucleic acids and free nucleotides and coenzymes.  Major antigens are carbohydrates in nature, e.g., blood group substance.  Biological role as a part of hormones and their receptors and enzymes.  Formation of glycolipid and glycoprotein both enter in structure of cell membrane Classification According to number of sugar units in molecule  Monosaccharaides (Simple sugar) → contain one sugar unit (Can’t be Hydrolyzed).  Disaccharides → contain two sugar units.  Oligosaccharide → contain 3 - 10 sugar units.  Polysaccharides → contain more than 10 sugar units. Monosaccharaides Classification 1- According to Functional group  Aldoses : monosaccharides containing aldehyde group (-CHO).  Ketoses: monosaccharides containing ketone group (-C=O). 2- According to number of carbon atom in molecule (3-7 C) Sugar No. of Carbons Includes Trioses 3 Aldotrioses and ketotrioses Tetroses 4 Aldotetroses and ketotetroses Pentoses 5 Aldopentoses and ketopentoses Hexoses 6 Aldohexoses and ketohexoses  Biochemistry Sugar derivatives 1- Sugar acids: - Are produced by oxidation of carbonyl carbon, last carbon or both. Carbonyl carbon Aldonic acid e.g. glucose gluconic acid. Last hydroxyl carbon uronic acid Glucose glucuronic acid BOTH Aldaric acids Glucose glucaric (saccharic) acid - Important in glucuronide formation and in glycosaminoglycans. & intermediates in uronic acid pathway HO CHO COOH CHO COOH OH H HC COHOH H C OH H C OH ater, H O2 HOHO HC2OC 2H H HO C O2 H HO C H OH HC COH H Nitric Dil. OH acid H CNitric Conc. OH acid H C OH OH H HC COHOH H C OH H C OH H2OH CHCH2OH 2OH COOH COOH ucose D-Glucose D-Gluconic acid D-Glucuronic acid D-Glucaric acid 2- Amino sugars: - these sugars, the hydroxyl group attached to C2 is replaced by an amino or an acetyl-amino group. 1) Amino sugars enter in glycoproteins , Glycosaminoglycans. 3- Deoxysugars: - Are produced by replacement of hydroxyl groups by hydrogen atom i.e. one oxygen is missed. - At C2: ribose gives deoxyribose that CHO CHO enters in structure of DNA. H C OH H C H - At C6 : L-galactose gives L-fucose H C OH H C OH that enter the structure of glycoproteins H C OH H C OH CH2OH CH2OH Ribose Deoxyribose  Biochemistry Starch Starch granule is formed of: - cereals, potatoes, 1) Starch gives blue color 1) Inner layer: called amylose. It legumes and with iodine. constitutes 15-20% of the granule other vegetables Amylopectin gives red and formed of non-branching color with iodine. - In plants it heIical structure of glucose units synthesized by 2) Partial hydrolysis linked together by α 1 — 4 photosynthesis. (digestion) by amylase glycosidic bond. enzyme gives various 2) Outer layer: called amylopectin forms of dextrins constitutes 80-85% of the granule and formed of branched chain. Each chain is composed of 24-30 glucose units linked together by α 1 — 4 glycosidic bond and a 1 — 6 glycosidic bond at branching points. Glycogen - Highly branched chain - The storage form - gives reddish violet - Each branch is composed of 12-14 of CHO in human color with iodine glucose units. and animals - Similar to amylopectin - in liver, muscles Cellulose - long linear chains of (β-D- - plants: vegetables, - give NO color with glucopyranose) linked together by cotton iodine - insoluble in β 1-4 glycosidic bond water - The presence of cellulose in diet - Cannot be digested due is important because it: to absence of digestive - increases the bulk of stool. hydrolase enzyme that - This stimulates intestinal attacks β-linkage. movement and prevents constipation. Complex carbohydrates Carbohydrates can be attached by glycosidic bonds to non-carbohydrate molecules including: 1- Purines and pyrimidines (in nucleic acids) 2- Proteins (in glycoproteins and proteoglycans) 3- Lipids (glycolipids) 4- Aromatic ring (in steroids and bilirubin)  Biochemistry Glycolysis  Definition :- means oxidation of glucose to give 2 molecules pyruvate 3C (in presence of oxygen) or 2 molecules lactate (in absence of oxygen).  Site :- Intracellular location ―cytosol‖ Glucose  Transport of glucose into cells :- Glucose Cytosol 1. Passive transport (facilitated diffusion) Sugars pass with concentration Glycolysis gradient i.e. from high to low concentration. It needs no energy. It occurs by means of Pyruvate sodium - independent facilitative transporter (GLUT) Mitochondria Acetyl Co-A  GLUT-1 :erythrocytes , blood–brain barrier Krebs cycle  GLUT-2 :in liver, kidney, pancreas. R. chain 2. Active transport 1. In cell membrane of intestinal cell , mobile carrier protein called sodium dependent glucose transporter (SGLT-2). it transport glucose to inside cell using energy  Stages :- 1. Stage one (the energy requiring stage): a) One molecule of glucose is converted into 2 molecules of glyceraldehyde-3- phosphates b) This step requires 2 molecules of ATP (energy loss) 2. Stage two (the energy producing stage): a) The 2 molecules of glyceraldehyde-3-phosphate are converted into pyruvate (aerobic glycolysis) or lactate (anaerobic glycolysis)  Biochemistry b) These steps produce ATP molecules (energy production)  Steps :- 1. Phosphorylation of glucose Hexokinase Glucose Glucose-6-phosphate & +2 Mg Glucokinase ATP ADP  Energy consuming & Regulatory step  Hexokinase : muscle and other tissues  Glucokinase: liver Hexokinase Glucokinase = Hexokinase IV Tissue distribution : In most Tissue distribution : In liver and tissues. pancrease Specificity : broad substrate Specificity : restricted substrate specificity specificity Kinetics parameter : low (Km) (high Kinetics parameter : high (Km) high affinity) Low V max (V max) Regulation : They are inhibited by Regulation : activity respond to change reaction product, glucose 6 - in glucose concentration Induced by phosphate. Constitutive insulin 2. Isomerization of glucose 6-phosphate Phosphohex Glucose-6-phosphate Fructose-6-phosphate ose 3. Phosphorylation of fructose 6-phosphate Phosphofru Fructose-6-phosphate Fructose 1,6 bisphosphate cto-kinase- +2 Mg ATP ADP  The most important control point -the rate-limiting and committed step of glycolysis 4. Cleavage of fructose 1,6-bisphosphate Aldolase Fructose 1,6 bisphosphate Dihydroxyacetone phosphate Glyceraldehyde-3-phosphate  Biochemistry Pyruvate dehydrogenase -Ketoglutarate Succinyl-COA Lipoic acid TPP FAD CO + NAD+ CoASH NADH + H 2  The reaction releases the second CO2  The reaction Produces the second NADH.  Inhibited by→ its products 1-NADH 2- succinyl CoA.  Activated by → Ca2+. 5. Cleavage of succinyl coenzyme A Succinate Thiokinase Succinyl-COA Succinate H2O CoASH GDP GTP ADP ATP 6. Oxidation of succinate Succinate Succinate Fumarate dehydrogenase FAD FADH2 7. Hydration of fumarate Fumarase Fumarate Malate H2O 8. Oxidation of malate ♲ Malate dehydrogenase Malate Oxaloacetate + NAD NADH+H +  Produces the third and final NADH of the cycle.  Regenerates oxaloacetat for another turn of the cycle. ♲  GENETICS  Phosphate group is attached to 5’ carbon of deoxyribose.  Nitrogenous base is attached to 1’ carbon of deoxyribose. Sugar-Phosphate Backbone  Phosphodiester bond → between 3’ carbon of deoxyribose and an oxygen atom of phosphate at 5’ carbon.  DNA strand has:  5’ end: with a free phosphate group  3’ end: with a free hydroxyl (OH) group   A molecule of DNA is composed of 2 long complementary polynucleotide chains coiled around one another to form Phosphodiester 3 a-double helix Bonds  The 2 chains are held together by hydrogen bonds binding the nitrogenous bases of the two chains : - 2 bonds between A = T - 3 bonds between C G  Thus there is an obligatory base pairing rules i.e. : If the bases sequence of one chain = T C A G C T The complementary chain should be = A G T C G A.  One end of a strand terminates with phosphate group (5s end) , the other end terminates with a free hydroxyl on carbon 3 of the sugar (3s end). The 2 strands are anti-parallel i.e. strands run in opposite direction DNA packaging  DNA is associated with proteins and is coiled to form chromatin.  GENETICS  Regulatory Elements :- Cis-acting & Trans-acting  Cis-acting :- Promoter & Enhancers & Silencers & Locus Control Region  ENHANCERS :- Distant DNA sequences that can enhance transcription of a specific gene  SILENCERS :- Distant DNA sequences that can inhibit transcription of a specific gene.  LOCUS CONTROL REGION (LCR) :- enhance transcription of a specific gene  Trans-acting :- Transcription Factors (TF)  TRANSCRIPTION FACTORS (TFs) :- DNA-binding regulatory proteins that bind to specific DNA sequences in promoter and other regulatory DNA sequences (enhancers, silencers), to initiate and regulate gene transcription.  General TFs →Required for all genes. & Bind to promoter sequences. & Allow RNA polymerase to bind to promoter region.  Specific TFs →Activate (or inhibit) only specific genes at specific times. Activators: bind to enhancers Repressors: bind to silencers Gene Expression  Production of normal RNA in the correct amount, in the correct place, and at the correct time during development or during the cell cycle.  Transcription → RNA Processing (modification) → Translation & Genetic Code “CENTRAL DOGMA” DNA ➔ RNA ➔ protein  DNA directs the synthesis & sequence of RNA.  RNA directs the synthesis & sequence of protein. Transcription  Process by which the information in a strand of DNA is COPIED into a molecule of RNA (mRNA) by RNA polymerase. (In Nucleus)  GENETICS  Principles :-  Only one of two DNA strands serves as a template for RNA synthesis.  Transcription relies on complementary base pairing.  RNA transcript is complementary to the template DNA strand.  Initial (primary) RNA transcript undergoes several processing reactions to make a mature mRNA.  Steps :-  INITIATION  TFs bind to promoter forming transcription initiation complex.  RNA polymerase II binds to transcription initiation complex. transcription starts at the transcription start site.  DNA strands are separated, giving RNA polymerase II access to the template strand.  RNA polymerase starts making mRNA by adding RNA nucleotides, which base-pair (complementary) with DNA nucleotides of template strand.  ELONGATION  RNA polymerase II leaves promoter region and moves along template strand , adding RNA nucleotides in the 5’ ➔ 3’ direction. (Direction of transcription, Polarity)  TERMINATION  Transcription proceeds till the DNA sequence that signals termination (unknown) is reached.  Both DNA and RNA are released from RNA polymerase II, and transcription is terminated.  Termination is associated with polyadenylation.  OSPE Anatomical plane Identify “mention name of anatomical plane” ← ‫ طريقة السؤال في االمتحان‬- Terms of movement Identify “mention name of movement” ← ‫ طريقة السؤال في االمتحان‬- Flexion Abduction Adduction Extension Medial Lateral rotation rotation Circumduction  OSPE Type of ossification Mention type of ossification ← ‫ طريقة السؤال في االمتحان‬-  Membranous ossification  Example :- skull cap “Vault” and clavicle  Cartilagenous ossification  Examples :- all other bones Vault clavicle Membranous ossification Cartilagenous ossification Structure of long bone Identify ← ‫ طريقة السؤال في االمتحان‬- 1. Diaphysis “Shaft”  Composed of compact bone 2. Epiphysis “Ends of bone”  Composed of spongy bone 3. Periosteum  outside covering of diaphysis 4. Arteries Supply bone cells with nutrients 5. Articular cartilage   Covers external surface of epiphyses 6. Medullary cavity   Cavity of the shaft  Contains yellow marrow & red marrow Compact bone Articular cartilage Cancellous Epiphyses Diaphysis bone  OSPE Nervous system Identify ← ‫ طريقة السؤال في االمتحان‬- Median longitudinal fissure Lt. hemisphere Rt. hemisphere Grey matter Lateral Ventricle Basal ganglia White matter  OSPE CELL ORGANELLES Identify & Mention labels ← ‫ طريقة السؤال في االمتحان‬- Intercellular Cell membrane space Cell membrane Cell membrane Cell coat Microvilli Cell membrane Cell coat (Microvilli)  OSPE A B C Nucleus (A) Nuclear pore (B) Nuclear membrane (C) Nucleolus E (D) Chromatin (E) Nuclear sap D C Hetero-chromatin (A) Peripheral chromatin (B) Island of chromatin (C) Peri-nuclear chromatin B A Lysosome containing Glycogen granules multiple vesicle (cell inclusions) (multi-vesicular body)  OSPE Epithelial tissue Mention type of epithelium ← ‫ طريقة السؤال في االمتحان‬- Simple squamous epithelium Simple cubical epithelium Simple columnar epithelium  OSPE Homeostasis  Definition :- means keeping conditions in internal environment constant = “Extracellular fluid” physically & chemically  For optimal cell function in human several conditions (important variables) in internal environment (extracellular fluid) must be maintained within narrow limits , These include: Stimulus  Body Temperature  Blood pressure  Blood pH Sensor  O2 and CO2concentration Receptors  Osmoregulation-Water balance  Blood glucose  Components of a homeostatic control system (Reflex arc) ?? Afferent 1. Stimulus  change in internal environment pathway 2. Sensor “receptor”  detects a change in variable (temperature, BP.) 3. Afferent pathway. 4. Integrating center  processes information and determines Integrating appropriate response. center 5. Efferent pathway. 6. Effector  produces response that counteract change or stimulus. Efferent  Types of homeostatic mechanisms ??? pathway 1- feed forward control system 2- positive feedback control system Effector 3- negative feedback control system Feed forward Mechanism Response  Body reacts before actual change affects variable (response in anticipation). Examples: 1) we wears heavy clothes when it is rainy before our body temperature changes. 2) Heart rate and breathing increase even before a person has begun the exercise. 3) we get thirsty while eating salty food, before blood concentration of NaCl has time to change.  OSPE LAB SAFTEY  BIOSAFETY LEVELS Mention biosafety levels ← ‫ طريقة السؤال في االمتحان‬- BL-1 agents are not known to cause disease BL-2 agents are associated with human disease BL-3 agents are associated with human disease and are potentially transmitted as aerosols BL-4 agents of life-threatening nature  NAME OF HAZARD Mention name of hazard ← ‫ طريقة السؤال في االمتحان‬-  OSPE  Identify micropipette  Identify  glass pipette  Uses  to transport a  Used  to transport a measured measured volume of liquid. volume of liquid.  Type  Fixed & Adjustable  Identify  Centrifuge  Identify  water bath  Used  to separate components of  Used  to incubate samples at a mixtures based on their size and density constant temperature over a long  It works using the sedimentation principle period of time  Identify  Spectrophotometer  Used  device used to measure amount of light absorbed to measures concentration of substance in sample Spectrometer ( producing light of selected color ) spectrophotometer Photometer (measuring intensity of light passing through tube)  OSPE BIOMOLECULES Benedict`s test used as test for reducing sugar  Benedict’s solution reacts with MOST saccharides that contain a reducing end ( a free ‫ــــ‬OH group). Except Sucrose (non-reducing sugar).  If a detectable carbohydrate is present, then the indicator changes color, based on how many carbs are present.  Benedict test : used to detect reducing sugars  Left to right: Benedict's reagent Degrees of reducing sugars  RESULTS:  Aqua-blue = negative.  Green to Yellow to orange = positive. Aqua blue Green Yellow Orange Iodine test used as test for detect starch IKI (IODINEIN POTASSIUM IODIDE) + starch ---> change in color  Iodine test : used to detect starch.  Left to right: IKI only starch solution starch solution + IKI.  RESULTS: Yellow-orange = negative. Purple-black = positive. Biuret test used as test for detect polypeptide “protein contain ≥3 amino acids”  Left to right: Biuret's reagent (BrR) water + BrR Protein( egg albumin) Protein (egg albumin + BrR) RES U LTS : Denim-blue = negative. Violet color = positive.  OSPE The Yellow Top Tube Additive  acid-citrate-dextrose (ACD) Mode of  Contains the active anticoagulant Action (ACD)  Used to obtain whole blood or plasma sample Laboratory tests  Blood group typing  HLA phenotyping  DNA study  Paternity testing The Lavender Top Tube Additive  Spray-dried K 2 EDTA (Di potassium Ethylene diamine tetra-acetic Acid)  Spray-dried K 3 EDTA (Tri potassium Ethylene diamine tetra-acetic Acid) Mode of  It contains EDTA as anticoagulant. Action  Forms calcium salts to remove calcium.  Used to obtain a whole blood or a plasma sample Laboratory  The whole blood sample is used for tests both:  Complete blood picture  Glycosylated hemoglobin (Hb A1c) The Blue Top Tube Additive  3.2% sodium citrate Mode of  Binds and remove calcium to prevent Action blood from clotting Laboratory  coagulation tests tests  Prothrombin Time (PT )  Partial Thromboplastin time (PTT)  OSPE DNA→RNA DNA→DNA RNA→RNA A→U A→T A→U C→G C→G C→G T→A Central Dogma In nucleus In cytoplasm 5ʹ 3ʹ 5ʹ DNA Transcription Translation DNA RNA 5ʹ 3ʹ 3ʹ 5ʹ 5ʹ 3ʹ Transcription Translation DNA DNA RNA 5ʹ 3ʹ 3ʹ  MCQ 34. The posterior part of hard palate is formed b. Nasal and ethmoid bones. of ………. c. Ethmoid and nasal bones. a. Palatine process of maxilla d. Vomer and ethmoid bones. b. Horizontal plate of palatine bone 40. Foramen magnum is bounded by …………. c. Perpendicular plate of palatine a. Lateral parts of occipital bone. bone b. Styloid parts of temporal bone. d. Pyramidal process of palatine bone c. Mastoid parts of temporal bone. 35. Motor root of trigeminal nerve passes d. Petrous parts of temporal bone. through ……… 41. The superior orbital fissure gives passage to a. Foramen ovale …….. b. Foramen lacerum a. Maxillary nerve c. Jugular foramen b. Optic nerve d. Anterior condylar foramen c. Trochlear nerve 36. A line at the level of the external occipital d. Facial nerve protuberance is ……….. 42. The cribriform plate is present within the a. Highest nuchal line ………. fossa. b. Superior nuchal line a. Infra-temporal c. Inferior nuchal line b. Anterior cranial 37. Ahmed has abnormal bony growth c. Middle cranial fossa compressing the jugular foramen structure. d. Posterior cranial fossa During examination, the doctor search for 43. Facial nerve passes through ……... the signs of the following cranial nerve a. External auditory meatus affection b. Internal auditory meatus a. The optic nerve and the nerves c. Superior orbital fissure controlling the extra-ocular d. Inferior orbital fissure muscles. 44. Between both occipital condyles there is b. The mandibular branch of the ………. trigeminal nerve. a. Foramen ovale c. The 7th and the 8th cranial nerves. b. Foramen spinosum d. The 9th, 10th and 11th cranial c. Sella turcica nerve. d. Foramen magnum 38. The foramen which is located between the 45. Type of joint of growth plate apex of petrous bone posteriorly, the a. Synovial joint pterygoid process anteriorly and the basilar b. Primary cartilaginous joint part of occipital bone medially is called: c. Secondary cartilaginous joint a. Foramen lacerum. d. Suture joint b. Jugular foramen. 46. What is between the greater and lesser wing c. Carotid canal. of sphenoid d. Foramen rotundum a. Infraorbital fissure 39. Bones making up the nasal septum are b. Supra orbital fissure …………. c. Foramen ovale a. Vomer and lacrimal bones. d. Carotid canal  MCQ Histology b. The nuclear envelope is formed from two membranes 1. Each of the following statements concerning c. There are two types of chromatin the nuclear envelope structure is true, d. The nors contains 4 chromosomes EXCEPT 6. In the nucleolus , pars fibrosa is formed of: a. Consists of two membranes a. Filaments of mRNA separated by the perinuclear space b. Granules of ribonucleoprotein b. Contains nuclear pores providing c. Nuclear sap communication between the d. Filaments of rRNA nucleus and cytoplasm 7. Euchromatin is characterized by being: c. Its outer membrane is studded with ribosomes a. Attached to the nucleolus d. Its outer membrane is continuous b. Condensed form of chromatin with golgi apparatus. c. Active chromatin 2. Each of the following statements concerning d. Form chromatin islands chromatin is true, EXCEPT: 8. Which of the following describe the nuclear a. Euchromatin is a lightly stained membrane structure and dispersed a. Three membrane layers b. Heterochromatin is a densely b. Two unit membranes without a stained and condensed space c. Heterochromatin takes part in c. One unit membrane with nuclear transcription pores d. Two types of chromatin may be d. Two unit membranes with a space transformed one into another 9. What is the peripheral Chromatin? 3. The outer nuclear membrane is continuous a. Heterochromatin associated with with.. nuclear envelope. a. Rough endoplasmic reticulum b. Heterochromatin scattered as b. Smooth endoplasmic reticulum chromatin granules in nuclear c. Golgi apparatus matrix. d. Cell membrane c. Heterochromatin surrounding the 4. Which of the following is true regarding nucleolus. nucleolus? d. Euchromatin a. Basophilic body in the cell center 10. All of the following is true regarding cell b. Consists of light and dark areas membrane EXCEPT: c. Consists of dense granules a. Is formed from phospholipids and glycolipids. d. Contains portions from 13,14,15,21 &22 b. It contains 3 hydrophilic layers. 5. All of the followings are true, EXCEPT c. Shows trilaminar appearance in EM. a. The nucleus is the largest organelles d. Contains peripheral proteins.  MCQ 19. Na+, and K+, Ca2+, and Cl− permeation a. They are synthesized from through their respective ion channels monomers. represents an example of: b. No structure within the polymer a. Passsive transport can repeat. b. Primary active transport c. Polymers are only oil-based chemicals. c. Secondary active transport d. A polymer can be made by a d. Phagocytosis rehydration reaction. 5. Which of the following best describes Biochemistry catabolism? a. It consumes energy. 1. What are the four major macromolecules of b. It is an endergonic reaction. life? c. It is used to build large molecules a. Carbohydrates, proteins, from small building blocks. polypeptides, synthetic fibers d. It is an exergonic reaction. b. Carbohydrates, polypeptides, polymers, synthetic fibers 6. Which of the phosphate groups releases the c. Carbohydrates, proteins, lipids and lowest energy when hydrolyzed from the nucleic acids ATP molecule? d. Proton, electron, neutron, photon a. First phosphate group b. Second phosphate group 2. Which of the following is the definition of c. Third phosphate group biochemistry? d. Both B and C a. It is a branch of life science that deals with the study of chemical 7. Which of the following is responsible for processes in nonliving organisms. specifying the 3D shape of a protein? b. It is a branch of life science that a. The peptide bonds deals with the study of the b. The amino acids sequence chemical processes in living c. Interaction with other polypeptides organisms. d. Interaction with molecular c. It is a branch of physical science chaperons that deals with physics in an 8. Amino acids with aromatic side chain are. inorganic world. a. Tryptophan, asparagine, tyrosine d. It is a branch of physical sciences b. Tryptophan, threonine, tyrosine that deals with physics in nonliving c. Phenylalanine, tryptophan, serine organisms. d. Phenylalanine, tryptophan, tyrosine 3. Which of the following is considered a 9. Which of the following amino acids must be macromolecule in biochemistry? supplemented in the diet? a. Vitamins a. Phenylalanine b. Minerals b. Cysteine c. Trace elements c. Glutamine d. Carbohydrates d. Asparagine 4. Which of the following is true regarding 10. Enzymes are polymers of: macromolecule polymers? a. Hexose sugar b. Amino acids  MCQ 33. Which of the following enzyme is 39. Which of the following cofactors is involved considered one of the regulatory enzymes in the conversion of pyruvate to acetyl- for glycolysis? CoA? a. Phosphofructokinase 1 a. Biotin, NAD+, and FAD b. Phosphofructokinase 2 b. NAD+, biotin, and TPP c. Aldolase c. Pyridoxal phosphate, FAD, and d. Enolase lipoic acid 34. Under anaerobic conditions oxidation of d. TPP, lipoic acid, and NAD+ mole of glucose yields __ moles of ATP 40. Number of protein complexes which are part a. One of ETC: b. Two a. 2 c. Eight b. 4 d. Nine c. 3 d. 5 35. How many moles of ATP produced at substrate level in glycolysis. 41. The succinate dehydrogenase step of TCA cycle produce ----------- ATP. a. One a. 1 b. Two b. 2 c. Four c. 3 d. Nine d. 4 36. How many molecules of ATP are produced 42. Before pyruvate enters the TCA cycle it by the total oxidation of acetyl CoA in TCA must be converted to---------------- cycle ? a. Acetyl CoA a. 6 b. Lactate b. 8 c. α-ketoglutarate c. 10 d. Citrate d. 12 43. The formation of citrate from oxaloacetate 37. Which of the following enzymes catalyze and acetyl CoA is------------ reaction. the substrate level phosphorylation step in a. Oxidation TCA cycle ? b. Reduction a. Isocitrate dehydrogenase c. Condensation b. Malate dehydrogenase d. Hydrolysis c. Aconitase 44. Choose the correct answer regarding d. Succinate thiokinase pyruvate dehydrogenase multienzyme complex? 38. Which of the following compound is a. In thiamin (vitamin B1) regenerated through tricarboxylic acid cycle deficiency, pyruvate formed in --------------- muscle cannot be transaminated to a. Pyruvate alanine. b. oxaloacetate b. In thiamin (vitamin B1) deficiency, c. α-ketoglutaric acid pyruvate formed in muscle cannot d. malate be carboxylated to oxaloacetate.  OSPE QUESTION STATION 1  Identify A  Identify B & mention 2 structure passing through it STATION 2  Identify A  Identify B STATION 3  Identify A “name of fossa”  Identify B & mention 2 structure passing through it Identify A Identify B  OSPE QUESTION Station 8  Identify A & mention age that ossifies it  Identify B & mention 2 muscle attached to it Station 9  Identify A  Mention muscle attached to fossa Station 10  Identify A  Mention 2 contents of fossa Station 11  Identify A & mention name at birth  Identify B  OSPE QUESTION station 17  Identify A  Identify part of long bone B Station 18  Mention type of joint A  Mention type of joint B Station 19  Mention type of joint A  Mention type of muscle B Station 20  Identify A  Identify B  Mention type of muscle C Station 21  Mention type of joint A  Mention type of muscle B  OSPE QUESTION Station 22  Mention type of joint A  Mention type of muscle B Station 23  Identify A  Identify B Station 24  Identify A  Identify B Station 25  Identify A  Identify B  OSPE QUESTION Station 35  Identify organelle  Identify A  Identify B Station 36  Mention type of epithelium Station 37  Mention type of epithelium Station 38  Mention type of epithelium  OSPE QUESTION Station 53  Mention biosafety levels Station 54 A. Mention the Biosafety level in each of the following labs: 1. A researcher works in a lab on an organism called Ebola virus. 2. A lab has a restricted entrance and eye wash station Station 55  Identify A & B A B Station 56  Identify A & B A B Station 57  Identify A & B A B  OSPE QUESTION Station 58  Identify A  Mention uses of B A B Station 59  Mention name of test  Mention uses of test Station 60  Mention name of test  Mention uses of test Station 60  Mention name of test  Mention uses of test Station 61  Mention name of test  Mention name of substance used for detection in test Station 62 A H 2O 2 2H2O + O2