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Questions and Answers
What is the non-protein part of haemoglobin?
How many polypeptide chains are present in haemoglobin?
What type of carbohydrates have 2-10 sugar units?
What is the definition of fatty acids?
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What are the products of hydrolysis of Maltose, Lactose, and Sucrose?
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What is the clinical importance of blood cholesterol?
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What are the types of lipoproteins classified based on density?
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What is the function of HDL?
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What is a known risk factor for Coronary Heart Disease?
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What is the term for the thickening or hardening of the arteries by a build-up of plaque in the inner lining of the artery?
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What is the composition of nucleosides?
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What is the difference between DNA and RNA?
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What is the action of endopeptidase?
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What is the end product of the urea cycle?
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What is nitrogen balance?
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What is the composition of ATP?
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What is the process by which an amino acid's amino group is transferred to a keto acid?
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What is the net energy yield during aerobic glycolysis?
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What is the enzyme that regulates glycogenolysis in the liver and muscles?
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What is the net energy yield from 1 Acetyl CoA during the TCA cycle?
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What is the process by which fatty acids are broken down to acetyl-CoA?
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What are the end-products of β-oxidation?
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What is the role of hormones in the regulation of blood glucose?
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What is the process by which DNA is converted to mRNA?
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Which of the following is an example of an acute-phase protein?
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What are the major plasma proteins present in blood?
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What is one of the primary functions of albumin in the blood?
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What is the major transport protein in blood that also contributes to immune responses?
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How is serum different from plasma?
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Which immunoglobulin exists as a pentamer?
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What is the major function of hemoglobin?
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Which type of bond links the heavy and light chains in an immunoglobulin?
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Which class of enzyme catalyzes the transfer of functional groups from one molecule to another?
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Which mechanism of enzyme action explains that the enzyme changes its shape when the substrate binds?
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Which class of enzyme catalyzes the conversion of one isomer into another?
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What factor typically decreases the rate of an enzymatic reaction after the optimum pH is reached?
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Which class of enzyme uses ATP to join two molecules together?
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What is the term for physically distinct forms of the same enzyme that catalyze the same biochemical reaction?
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Which type of enzymatic inhibition involves binding to the enzyme-substrate complex?
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Which of the following enzymes catalyzes hydrolysis reactions?
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Study Notes
Coronary Heart Disease Risk Factors
- High levels of LDLC (> 130 mg/dL) and low levels of HDLC (< 40 mg/dL) are known risk factors for Coronary Heart Disease.
- Other risk factors include obesity, hypertension, diabetes mellitus, smoking, and stress.
Atherosclerosis
- Atherosclerosis is the thickening or hardening of the arteries by a build-up of plaque in the inner lining of the artery.
Fatty Liver Disease
- Fatty liver disease is a condition caused by excessive fat build-up in the liver.
Nucleic Acids
- Nucleic acids are complex organic molecules consisting of many nucleotides linked in a long chain.
- The two-ringed nitrogenous bases are adenine and guanine.
- The single-ringed nitrogenous bases are cytosine, thymine, and uracil.
- Nucleosides are composed of a nitrogenous base and a pentose sugar (either ribose or deoxyribose).
- Nucleotides are composed of a nitrogenous base, a pentose sugar, and phosphate groups esterified to the sugar.
- ATP (adenosine triphosphate) is composed of adenine, ribose, and three phosphate groups.
DNA and RNA
- DNA is double-stranded, while RNA is single-stranded.
- The nitrogenous bases present in DNA are adenine, guanine, cytosine, and thymine.
- The nitrogenous bases present in RNA are adenine, guanine, cytosine, and uracil.
Nitrogen Balance
- Nitrogen balance refers to the balance between nitrogen intake through the diet and nitrogen excretion from the body.
Protein Structure and Function
- Endopeptidases break internal peptide bonds in proteins, while exopeptidases cleave amino acids on the terminal end of protein molecules.
- Urea is the end product of the urea cycle.
- Decarboxylation, transamination, and deamination are processes involved in protein metabolism.
- Acute-phase proteins include C-reactive protein, heptoglobin, fibrinogen, and α-1 antitrypsin.
Plasma Proteins
- The major plasma proteins present in blood are albumin, globulins, and fibrinogen.
- Albumin functions in colloidal osmotic pressure, transport, nutrition, and buffering.
- Globulins are involved in the immune system and transport.
- Fibrinogen is involved in blood coagulation and can form an insoluble fibrin clot.
Serum and Plasma
- Plasma is the liquid portion of blood that remains after clotting, while serum is the liquid portion of blood that remains after clotting and the removal of fibrinogen.
- Albumin is the fastest-moving protein during electrophoresis.
Immunoglobulins
- Immunoglobulins are glycoproteins that recognize, bind, and destroy specific antigens.
- The major types of immunoglobulins are IgA, IgD, IgE, IgG, and IgM.
- Immunoglobulins have a basic structure consisting of four polypeptide chains (two light and two heavy chains).
- Disulfide bonds link the heavy and light chains in an immunoglobulin.
- IgA exists as a dimer, while IgM exists as a pentamer.
Hemoglobin and Myoglobin
- Hemoglobin is a tetrameric oxygen transport protein found in red blood cells.
- Myoglobin is a monomeric oxygen transport protein found in muscles.
- The two major functions of hemoglobin are the transport of oxygen from the lungs to the tissues and the transport of carbon dioxide from tissues to the lungs for excretion.
- The two major functions of myoglobin are the storage of oxygen and the supply of oxygen to the cells in muscles.
Enzymes
- Transferases catalyze the transfer of functional groups from one molecule to another.
- Hydrolases catalyze hydrolysis reactions.
- Lyases catalyze the addition of a group to a double bond or the removal of a group to form a double bond.
- Isomerases catalyze the conversion of one isomer into another.
- Ligases catalyze the joining of two molecules using ATP for energy.
- Isozymes are physically distinct forms of the same enzyme that catalyze the same biochemical reaction.
- Examples of isozymes include lactate dehydrogenase and creatine kinase.
Enzyme Mechanisms
- The four major mechanisms of action for enzymes are lowering activation energy, Michaelis-Menten theory, Fischer's lock and key hypothesis, and Koshland's induced fit theory.
- Koshland's induced fit theory explains that the enzyme changes its shape when the substrate binds.
- Competitive inhibition occurs when the inhibitor binds to the active site, while non-competitive inhibition occurs when the inhibitor binds to the allosteric site.
- Uncompetitive inhibition occurs when the inhibitor binds to the E-S complex.
Factors Influencing Enzymatic Reactions
- Factors influencing enzymatic reactions include temperature, pH, substrate concentration, enzyme concentration, presence of inhibitors, presence of activators, presence of repressors, availability of co-enzymes, and covalent modification.
Hemoglobin Structure
- Hemoglobin is composed of a protein part (globin) and a non-protein part (heme).
- Heme is composed of protoporphyrin IX with four methyl groups, two propionyl groups, two vinyl groups, and an iron atom.
- Adult hemoglobin (HbA1) is made up of two α-chains and two β-chains (α2β2).
Clinical Conditions
- Low hemoglobin levels are associated with various clinical conditions.
- Hypocholesterolemia and hypercholesterolemia are clinical conditions associated with blood cholesterol levels.
Carbohydrates
- Examples of monosaccharides include glucose, fructose, and galactose.
- Examples of disaccharides include maltose, lactose, and sucrose.
- Examples of polysaccharides include glycogen, starch, and cellulose.
- Oligosaccharides are carbohydrates having 2-10 sugar units.
- Polysaccharides are carbohydrates having more than 10 sugar units.
Fatty Acids
- Fatty acids are aliphatic carboxylic acids with a hydrocarbon chain.
- Fatty acids can be classified based on the nature of the hydrocarbon chain and nutritional status.
- Examples of essential fatty acids include linoleic acid, linolenic acid, and arachidonic acid.
- Examples of non-essential fatty acids include palmitic acid and stearic acid.
Lipoproteins
- Lipoproteins are classified into five major types based on density: chylomicrons, VLDL, IDL, LDL, and HDL.
- HDL functions in the transport of cholesterol from peripheral tissues to the liver.
- LDL functions in the transport of cholesterol from the liver to peripheral tissues.
Cholesterol
- The clinical importance of blood cholesterol levels includes hypocholesterolemia and hypercholesterolemia.
- The clinical importance of HDL and LDL cholesterol levels includes their role in cardiovascular disease.
Protein Metabolism
- Decarboxylation, transamination, and deamination are processes involved in protein metabolism.
- Biologically important compounds synthesized from amino acids include glutathione, melatonin, serotonin, creatine, and nitric oxide.
Glycolysis and Gluconeogenesis
- Glycolysis is the process in which glucose undergoes breakdown to produce pyruvate or lactate under aerobic or anaerobic conditions.
- Gluconeogenesis is the process in which glucose is synthesized from non-carbohydrate sources.
- Glycogenolysis is the process in which glycogen undergoes breakdown to produce glucose.
- Glycogen phosphorylase is the enzyme that regulates glycogenolysis in the liver and muscles.
- Glycogenesis is the process in which glycogen is synthesized from glucose.
Energy Yield
- The net energy yield during aerobic glycolysis is 7 ATPs.
- The net energy yield during anaerobic glycolysis is 2 ATPs.
- The net energy yield from 1 Acetyl CoA during the TCA cycle is 3 NADH, 1 FADH2, and 1 ATP.
Hormones and Blood Glucose
- Hormones play a crucial role in the regulation of blood glucose levels.
Beta-Oxidation
- Beta-oxidation is the process by which fatty acids are broken down to acetyl-CoA.
- The end-products of beta-oxidation are acetyl-CoA, FADH2, and NADH.
Fatty Acid Synthesis
- The precursors for fatty acid synthesis are acetyl-CoA and NADPH.
Ketone Bodies
- Examples of ketone bodies include acetone, acetoacetate, and beta-hydroxybutyrate.
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