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Questions and Answers

What is the non-protein part of haemoglobin?

Polypeptide

Haem

Heme (correct)

Protoporphyrin IX

How many polypeptide chains are present in haemoglobin?

4 (correct)

What type of carbohydrates have 2-10 sugar units?

Disaccharides

Polysaccharides

Oligosaccharides (correct)

Monosaccharides

What is the definition of fatty acids?

Aliphatic carboxylic acids with a hydrocarbon chain Signup and view all the answers

What are the products of hydrolysis of Maltose, Lactose, and Sucrose?

Glucose and Fructose Signup and view all the answers

What is the clinical importance of blood cholesterol?

Hypocholesterolemia and Hypercholesterolemia Signup and view all the answers

What are the types of lipoproteins classified based on density?

Chylomicrons, VLDL, IDL, LDL, and HDL Signup and view all the answers

What is the function of HDL?

Transporting cholesterol from peripheral tissues to liver Signup and view all the answers

What is a known risk factor for Coronary Heart Disease?

High levels of LDLC Signup and view all the answers

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?

Atherosclerosis Signup and view all the answers

What is the composition of nucleosides?

Nitrogenous base, pentose sugar Signup and view all the answers

What is the difference between DNA and RNA?

DNA is double-stranded, RNA is single-stranded Signup and view all the answers

What is the action of endopeptidase?

Break internal peptide bonds in the protein Signup and view all the answers

What is the end product of the urea cycle?

Urea Signup and view all the answers

What is nitrogen balance?

The balance between nitrogen intake and nitrogen excretion Signup and view all the answers

What is the composition of ATP?

Adenine, ribose, and three phosphate groups Signup and view all the answers

What is the process by which an amino acid's amino group is transferred to a keto acid?

Transamination Signup and view all the answers

What is the net energy yield during aerobic glycolysis?

7 ATPs Signup and view all the answers

What is the enzyme that regulates glycogenolysis in the liver and muscles?

Glycogen phosphorylase Signup and view all the answers

What is the net energy yield from 1 Acetyl CoA during the TCA cycle?

3 NADH, 1 FADH2, 1 ATP Signup and view all the answers

What is the process by which fatty acids are broken down to acetyl-CoA?

β-oxidation Signup and view all the answers

What are the end-products of β-oxidation?

Acetyl CoA, FADH2, NADH Signup and view all the answers

What is the role of hormones in the regulation of blood glucose?

To regulate blood glucose levels Signup and view all the answers

What is the process by which DNA is converted to mRNA?

Transcription Signup and view all the answers

Which of the following is an example of an acute-phase protein?

C-reactive protein Signup and view all the answers

What are the major plasma proteins present in blood?

Albumin, globulins, and fibrinogen Signup and view all the answers

What is one of the primary functions of albumin in the blood?

Colloidal osmotic pressure Signup and view all the answers

What is the major transport protein in blood that also contributes to immune responses?

Globulin Signup and view all the answers

How is serum different from plasma?

Serum lacks fibrinogen Signup and view all the answers

Which immunoglobulin exists as a pentamer?

IgM Signup and view all the answers

What is the major function of hemoglobin?

Oxygen transport from lungs to tissues Signup and view all the answers

Which type of bond links the heavy and light chains in an immunoglobulin?

Disulfide bonds Signup and view all the answers

Which class of enzyme catalyzes the transfer of functional groups from one molecule to another?

Transferases Signup and view all the answers

Which mechanism of enzyme action explains that the enzyme changes its shape when the substrate binds?

Koshland’s induced fit theory Signup and view all the answers

Which class of enzyme catalyzes the conversion of one isomer into another?

Isomerases Signup and view all the answers

What factor typically decreases the rate of an enzymatic reaction after the optimum pH is reached?

Denaturation of the enzyme Signup and view all the answers

Which class of enzyme uses ATP to join two molecules together?

Ligases Signup and view all the answers

What is the term for physically distinct forms of the same enzyme that catalyze the same biochemical reaction?

Isoenzymes Signup and view all the answers

Which type of enzymatic inhibition involves binding to the enzyme-substrate complex?

Uncompetitive inhibition Signup and view all the answers

Which of the following enzymes catalyzes hydrolysis reactions?

Protease Signup and view all the answers

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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