This exam combines questions from exams given during past years. Remember that the final exam will also include nine of the online practice questions. The correct answer, relative Objective, and percent of the class answering each question correctly is at the end of the examination. The mean score for the entire exam is also listed. The mean score is in the middle of the B range.

1. 7.4
2. 7.2
3. 7.1
4. 7.7
5. 6.4

1. An equal amount of ammonia and ammonium ion
2. Ten times more ammonia than ammonium ion
3. One hundred times more ammonia than ammonium ion
4. Ten times more ammonium ion than there is ammonia
5. One hundred times more ammonium ion than there is ammonia

1. CO₂
2. Alanine
3. NH₄Cl
4. NaHCO₃
5. Ascorbic acid

1. Decrease of [H⁺] in blood
2. Decrease of [HCO₃^-] in blood
3. Decrease of [H₂CO₃] in blood
4. Decrease of pCO₂ in blood
5. Decrease of dissolved CO₂ in blood

1. Row A
2. Row B
3. Row C
4. Row D
5. Row E

1. Row A
2. Row B
3. Row C
4. Row D
5. Row E

1. Glutamate
2. Histidine
3. Methionine
4. Cysteine
5. Cystine

1. Alanine at a pH of 11.0
2. Arginine at a pH of 10.0
3. Histidine at a pH of 8.0
4. Tryptophan at a pH of 5.0
5. Glutamine at a pH of 1.0

1. Glutamate: Positively charged at a pH of 7.4
2. Histidine: Positively charged at a pH of 4.1
3. Lysine: No charge at a pH of 3.8
4. Aspartate: Negatively charged at a pH of 1.7
5. Arginine: Negatively charged at a pH of 6.0

NH₃⁺-Ala-Phe-Glu-Lys-Arg-Pro-COO^-

1. +2
2. 0
3. +1
4. -1
5. -2

1. Quaternary structure
2. Mosaic
3. Motif
4. Domain
5. Native Protein

1. her amyloid protein is made from starch
2. electrophoresis reveales a P-protein (polyclonal-protein)
3. she has extracellular deposition of insoluble fibrillar protein
4. The amyloid protein is 100% beta-turns
5. The amyloid protein is 100% alpha-helix

1. The formation of a fibrous polymer after oxygen saturation of HbF
2. Each HbF can develop one hydrophobic interaction with another HbF
3. The formation of fibrous polymers increases the plasticity of the red blood cell
4. More HbF initiates weaker oxygen binding which, in turn, initiates polymerization
5. Each deoxygenated HbS expresses a hydrophobic pocket

1. Occur rarely in nature
2. Involves two antiparallel chains
3. Includes zinc atoms bound to cysteine and histidine residues
4. Hydrogen bonds between oxygens and nitrogen atoms four residues apart
5. Coils rich in proline residues

1. hemoglobin electrostatically bound to galactose
2. synthesized only in the kidney, liver, and pancreas
3. made by the enzyme glucohemoloobin synthase
4. made during protein synthesis
5. a measure of blood glucose during the past 6 weeks

1. Aspartate is substituted for cysteine on HbS subunits
2. Red blood cells are usually only "sickle" shaped in tissue capillaries
3. The "anemia" is from an iron deficiency
4. Amino acid substitution results in a hydrophobic knob or area
5. "Pain" associated with this disease is from vessel wall injury

1. Two electrons and two protons are transferred to NAD⁺
2. Two electrons and two protons are transferred from NAD⁺
3. One electron and two protons are transferred to NAD⁺
4. One electron and two protons are transferred from NAD⁺
5. Two electrons and one protons are transferred to NAD⁺

1. The conversion of urate to hypoxanthine
2. The conversion of urate to xanthine
3. The conversion of hypoxanthine to inosine monophosphate
4. The conversion of guanine to guanosine monophosphate
5. The conversion of GMP to urate

1. Initial energy state
2. Activation energy
3. Net energy change
4. The Vmax
5. Final energy state

1. Calmodulin
2. Troponin I 
3. Protein kinase A
4. Zymogen
5. Protein phosphatase

1. decrease the Km and decrease the Vmax
2. decrease the Km, but not the Vmax
3. always just change the Vmax
4. increase the Km but not change the Vmax
5. increase the Km and decrease the Vmax

1. competitive inhibition
2. that an allosteric activator is absent
3. that the enzyme is phosphorylated
4. Michaelis-Menten kinetics
5. cooperative binding

1. A phosphorylated tyrosyl residue
2. A phosphorylated seryl residue
3. A src homology binding domain (SH2 domain)
4. Bound inositol trisphosphate
5. An alpha-1 receptor

1. The receptor binds to the IRS-protein
2. The receptor inhibits phospholipase-C
3. The endoplasmic reticulum releases calcium ions
4. There is a reduction in the diacylglycerol concentration
5. Calmodulin dissociates from all the proteins to which it normally binds

1. little calcium released near the presynaptic membrane
2. many inhibitory proteins in the neuromuscular junction
3. much vesical fusion in the presynaptic junction
4. much acetylcholine esterase
5. few acetylcholine receptors in the postsynaptic membrane

A + H₂0 = B + C Delta-G^o' = + 11 kcal/mol
D + H₂0 = B + G Delta-G^o' = + 3 kcal/mol
K + H₂0 = B + L Delta-G^o' = -7 kcal/mol
J + H₂0 = B + M Delta-G^o' = -5 kcal/mol

Which of these reactions would be exergonic when proceeding from left to right?

1. A + G = C + D
2. A + M = C + J
3. D + M = G + J
4. A + L = K + C
5. K + M = J + L

1. Oxidoreductases
2. Transferases
3. Hydrolases
4. Lyases
5. Ligases

1. Without oxygen, the electron transport system is inhibited
2. Without oxygen, a proton gradient could not be maintained
3. Without oxygen, an adequate amount of oxidative phosphorylation can not occur
4. Without oxygen, there will not be enough ATP to cause adequate muscle contraction
5. Without oxygen, intracellular calcium concentrations cannot be maintained.at a high enough level

1. The reaction will be at equilibrium
2. The reaction will proceed from right to left
3. The Delta G^o' will become more negative
4. The Delta G will become more negative
5. The Delta G^o' will become more positive

1. Most of the water produced in our body is from the oxidation of carbohydrates
2. Most of the water produced in our body is from the oxygen we breathe
3. Most of the CO₂ we exhale is produced by glycolysis
4. Most of the CO₂ we exhale is produced by beta-oxidation of fatty acids
5. Most of the CO₂ we exhale is produced from oxygen in the electron transport chain

1. The process of oxidative phosphorylation refers to the electrochemical gradient used for the synthesis of the high energy bond of ATP
2. Oxidative phosphorylation is an example of an aerobic pathway
3. Substrate level phosphorylation is particularly important for converting fuel energy to ATP in red blood cells
4. Oxidative phosphorylation stops if oxygen is removed
5. The generation of ATP during the conversion of glucose to lactate is an example of oxidative phosphorylation

1. Alpha-ketoglutarate in the TCA cycle requires thiamin
2. Glucose-6-phosphate dehydrogenase has an absolute requirement for thiamin
3. Pyruvate carboxylase has a requirement for thiamin
4. Thiamin is an intermediate in the electron transport chain
5. Myosin ATPase has an absolute requirement for thiamin

1. The ADP concentration increases
2. The proton gradient across the mitochondrial membrane is diminished
3. The electron transport chain produces more water
4. The concentration of NADH decreases and the concentration of NAD⁺ increases
5. Alpha-ketoglutarate dehydrogenase is inhibited by phosphorylation

1. Is found in the cytosol
2. Is controlled by calcium ion, the ADP/ATP ratio, and the NADH concentration
3. Is also called the Cori cycle
4. Consumes most of the CO₂ produced by ribosomes
5. Produces most of the water made in humans

1. These are enzymes which remove electrons in the form of hydrogen from various structures and transfer them to others
2. At least one catalyzes the "rate-limiting steps" of the TCA cycle
3. GTP is generated from one of them via substrate level phosphorylation
4. NAD⁺ and FAD are the electron-accepting coenzymes for these enzymes
5. At least one catalyzes a reversible reactions

1. Inhibited by increases in the calcium concentration.
2. Activated by increased in acetyl CoA
3. Activated by increases in NADH
4. Activated by increases in ADP
5. Inhibited by increases in AMP

1. Rate of production of succinate
2. Rate of production of NADH
3. Concentration of alpha-ketoglutarate and pyruvate
4. Production of ATP
5. Production of FADH₂

1. Increased Ca⁺⁺ will cause dephosphorylation and activation of the enzyme
2. Increased ADP will inhibit phosphorylation of the enzyme and activate the enzyme
3. Increased ADP will activate ATP synthase and lower the proton gradient
4. A lower proton gradient will increase the utilization of NADH
5. Increased NADH will activate pyruvate dehydrogenase

1. Complex I
2. Complex II
3. Complex III
4. Cytochrome C
5. Complex IV

1. The inner mitochondrial membrane is impermeable to protons
2. The cytosol has a higher pH than the matrix
3. In the absence of a proton motive force, ATP will not be synthesized
4. The electrochemical potential comes from both the electrical potential and the proton concentration gradient
5. Electrons are passed from one carrier to the next as protons are pumped across the inner mitochondrial membrane

1. It becomes uncoupled
2. More ATP is made
3. The concentration of NADH increases
4. The cytochromes are all oxidized
5. The pumping of protons increases resulting in an increase in the proton gradient.

1. Causes "uncoupling" of oxidative phoshorylation
2. Passes electrons from NADH directly to O2
3. Creates an excess of ATP
4. Does not effect energy metabolism
5. All of the above

1. An inhibitor of cyt a + a₃
2. An inhibitor of complex I
3. An inhibitor of complex II
4. An inhibitor of complex III
5. A proton ionophore

1. 3 ATPs
2. 4 ATPs
3. 5 ATPs
4. 7 ATPs
5. 10 ATPs

1. Glucose from the sucrose is catabolized aerobically by bacteria
2. Aerobic metabolism of glucose produces hydroxyapatite like crystals which are imperfect
3. Anaerobic metabolism produces pyruvate which is basic and attacks hydroxyapatite
4. Aerobic metabolism produces pyruvate which raises the pH about 9.0. This pH dissolves teeth
5. Anaerobic metabolism produces lactate and lowers the pH below 5.0. Acid dissolves bone

1. Glucose
2. Lactate
3. Galactose
4. Pyruvate
5. Alanine

1. a decrease in insulin that, in turn, increases anaerobic glycolysis in the brain
2. a decrease in oxidative phosphorylation so the cells have to rely upon anaerobic glycolysis
3. a decrease in the oxidation of tyrosine to epinephrine which decreases gluconeogenesis in muscle
4. a decrease in the removal of CO₂ from the blood. The resulting decrease in pH causes an increase in glycolysis in most cells
5. an increase in glycolysis in red blood cells

1. PPi
2. Acyl CoA
3. ATP
4. CoA
5. ADP

1. Free fatty acid synthesis is increased
2. Malonyl CoA inhibits carnitine palmitoyl transferase I
3. The concentration of blood albumin increases
4. More fatty acid transporters appear on the surface of liver cells
5. More triacylglycerol is hydrolyzed in adipose cells

1. As independent water soluble compounds in the blood
2. By using receptors on red blood cells
3. Bound to serum proteins
4. Free fatty acids do not travel to liver
5. By using enzymes that modify them

1. The formation of propionyl CoA could lead to the production of glucose from B-oxidation
2. The formation of acetyl CoA could lead to ketone bodies synthesis
3. Acetyl CoA could be converted to pyruvate allowing for the production of glucose
4. Acetyl CoA could be used for the synthesis of HMG CoA
5. Acetyl CoA might be oxidized by the TCA cycle

1. Fatty acid synthesis in adipose tissue
2. Beta-oxidation in liver
3. Malonyl CoA concentrations in liver
4. Protein synthesis in muscle
5. Glycogenolysis in muscle

1. Glucagon would be increased
2. Free fatty acid concentration would be normal
3. C-peptide concentration would be increased
4. Epinephrine concentration would be normal
5. Concentration of glucose would be normal

1. Her blood insulin will not be in the normal range
2. Her beta-cells are secreting enough insulin
3. Her muscle cells are responding normally to insulin
4. Her adipose cells are responding normally to insulin
5. Her rate of gluconeogenesis is abnormal

1. The active form of insulin is composed of two polypeptide chains linked by two interchain disulfide bonds
2. The A-Chain has an intrachain disulfide bond
3. Insulin is synthesized as a preprohormone which is converted to proinsulin
4. Stimulation of A-cells by glucose causes exocytosis of the insulin storage vesicles
5. Cleavage of proinsulin to insulin yields a C-peptide

1. Increased glucose transport into muscle
2. Decreased glycogen phosphorylase activity in muscle
3. Decreased gluconeogenesis in liver
4. Increased glucose uptake into brain
5. Decreased glycogen phosphorylase in liver

1. The phosphorylation of glucose
2. The formation of UDP-glucose
3. The actions of the enzyme glycogen synthase, activated by the hormone glucagon
4. The actions of a branching enzyme, to ensure branching
5. The conversion of glucose-6-phosphate to glucose-1-phosphate by the enzyme phosphoglucomutase

1. In both skeletal muscle and liver, the glucose-6-phosphate formed enters the glycolytic pathway
2. Glycogen is an important fuel source for skeletal muscle when ATP demands are low
3. Glycogen in skeletal muscle is produced by gluconeogenesis during a prolonged fast
4. Liver glycogen is the first and immediate source of glucose for the maintenance of blood glucose levels
5. The pathways of glycogenolysis and gluconeogenesis in a liver cell are not activated together

1. Dephosphorylation and inactivation of glycogen phosphorylase
2. Phosphorylation and activation of glycogen synthase
3. Dephosphorylation and activation of glycogen synthase
4. Phosphorylation and activation of glycogen phosphorylase
5. Phosphorylation and inactivation of glycogen phosphorylase

1. Is activated by malonyl CoA
2. Requires AMP
3. Produces malate as a product
4. Requires biotin as a cofactor
5. Is inhibited by CO₂

1. hexokinase
2. fructose-2, 6-bisphosphatase
3. glucokinase
4. glucose-6-phosphatase
5. fructose-1, 6-bisphosphatase

1. oxidized by NADH to form oxaloacetate
2. reduced by NADH to form oxaloacetate
3. oxidized by NAD+ to form pyruvate
4. reduced by NAD+ to form pyruvate

1. Cytosolic concentration of ribose-1-phosphate
2. Mitochondrial concentration of ribose-5-phosphate
3. Concentration of glyceraldehyde-3-phosphate
4. Concentration of NADPH in the cytosol
5. Concentration of NAD⁺ in the endoplasmic reticulum

1. Oxidizing vitamin C
2. Oxidizing vitamin E
3. Oxidizing glutathione
4. Reductive biosynthesis of fatty acids
5. Beta-oxidation of fatty acids

1. Glutathione reductase
2. Phosphoglucoisomerase
3. Glucose-6-phosphate dehydrogenase
4. 6-phosphogluconate dehydrogenase
5. Gluconolactonase

1. 100% from gut
2. 100% from gluconeogenesis
3. 100% from glycogenolysis
4. 50% from gut and 50% from gluconeogenesis
5. 50% from glycogenolysis and 50% from gluconeogenesis

1. Tissues use the same amount of glucose that they use during a brief fast
2. Blood glucose levels decrease drastically during a four-week fast
3. As a fast progresses, tissues rely predominantly on fuels derived from adipose triacylglycerols
4. Blood ketone levels decrease dramatically after 3-5 days of fasting
5. After 3-5 days of fasting, the brain increases its utilization of glucose and the rate of gluconeogenesis and the production of urea increases

1. Glucose from the diet
2. Gluconeogenesis only
3. Glycogenolysis only
4. Both gluconeogenesis and glycogenolysis
5. Glucose from the diet, gluconeogenesis, and glycogenolysis

1. linoleic
2. palmitic
3. oleic
4. stearic
5. palmitoleic

1. Ethanolamine from diacylglycerol
2. Phosphatidylcholine from diacylglycerol and CDP-choline
3. Phosphatidylcholine from phosphatidylethanolamine
4. Phosphatidylethanolamine from phosphatidylserine
5. Phosphatidylserine from phosphatidylethanolamine

1. Endoplasmic reticulum
2. Golgi complex
3. Lysosome
4. Cytosol
5. None of the above

1. Dipalmitoylphosphatidylcholine
2. Phosphatidyl glycerol
3. Surface active proteins
4. Lung surfactant
5. Sphingomyelin

1. Uses activated hexokinase
2. Is inhibited by glucose
3. Is inhibited by insulin
4. Uses activated glycogen phosphorylase
5. Is inhibited by high cAMP

1. Capillaries don't have as much lipoprotein lipase activity
2. Adipose hormone sensitive lipase is more active
3. More VLDL is being synthesized in the liver
4. The cyclic-AMP concentration of adipose tissue is high
5. Brain usage of free fatty acids is down

1. Less serum lipoproteins
2. Lower blood glucose
3. Decreased production of lipoprotein by the liver
4. Decreased lipoprotein lipase activity
5. Decreased hormones sensitive lipase activity

1. Stimulation of acetyl CoA carboxylase
2. Stimulation of the lipolytic activity of hormone sensitive lipase (HSL)
3. Stimulates adipose cells to synthesize and secrete LPL (lipoprotein lipase)
4. Stimulates the enzyme glucose-6-phosphate dehydrogenase
5. Increase in the number of glucose transporters in adipose cell membranes

1. NAD⁺
2. Acetyl CoA
3. Pyridoxal phosphate (PLP)
4. FADH₂
5. NADPH

1. Low protein diet
2. Antibiotics
3. Lactulose
4. Enemas
5. Low carbohydrate diet

1. Argininosuccinase
2. Argininosuccinate synthetase
3. Ornithine transcarbamoylase
4. Arginase

1. Pyruvate
2. alpha-ketoglutarate
3. Oxaloacetate
4. Methionine
5. Carbamoyl phosphate

1. Glutamine
2. Proline
3. Methionine
4. Cysteine
5. Asparagine

1. Of vitamin B₁₂
2. Of folic acid
3. A deficiency in the pathway that synthesizes methyl cobalamin
4. A deficiency in the pathway that synthesizes N⁵-methyl tetrahydrofolate
5. All of the above

1. Pyruvate
2. Oxaloacetate
3. Succinyl CoA
4. Acetyl CoA
5. Fumarate

1. Methionine
2. Serine
3. Cystathionine
4. Homocystine
5. Cystine

1. Deep, rapid breathing causes a decrease in the partial pressure of carbon dioxide (PaCO₂) in the blood.
2. The removal of carbon dioxide through deep, rapid breathing results in a rise in the blood pH
3. When endogenous acid production rises sharply, net acid excretion cannot keep pace and the bicarbonate lost in buffering is not replaced causing plasma HCO₃^- levels to fall
4. Serum bicarbonate levels will decrease after the administration of an insulin injection
5. The fall in insulin causes fat cells to liberate fatty acids, which flood the hepatocytes

1. Glutamine for valine
2. Valine for glutamate
3. Hydrophobic amino acid for another hydrophobic amino acid
4. Hydrophilic amino acid for another hydrophilic amino acid
5. Hydrophilic amino acid for a hydrophobic amino acid

Aldolase is classified as a(n)

1. Oxidoreductase
2. Transferase
3. Hydrolase
4. Lyase
5. Isomerase

When the blood concentration of insulin is increases, less glucagon is produced and there is a(n)

1. Increases in the activity of adenylate cyclase
2. Increase in the activity of cAMP phosphodiesterase (3’, 5’-phosphodiesterase)
3. Increase in binding of cAMP to the inhibitory subunits of protein kinase A
4. Increase in cAMP
5. Increase in protein kinase A activity

1. Muscle needs ATP to contract
2. Most ATP is produced by oxidative phosphorylation
3. NADH and FADH2 are produced by the TCA cycle
4. The TCA cycle needs thiamine pyrophosphate to function
5. A shortage of thiamine results in the inability to oxidize NADH

In the muscle, all of the following are part of the pathway whereby increased epinephrine causes an increase in the glycolytic pathway EXCEPT

1. Increased binding of GTP to G-protein
2. Activation of the cAMP cascade
3. Increased phosphorylation of enzymes by protein kinase A
4. Activation of fructose-2,6-bisphosphatase and inhibition of phosphofructokinase-2
5. Increased binding of fructose-2,6-bisphosphate to phosphofructokinase-1

All of the following help to explain the mechanism for releasing insulin from beta-cells in response to the concentration of blood glucose - EXCEPT

1. The important regulator of glycolysis in beta cells is the concentration of glucose reacting with glucokinase
2. ATP is made in proportion to the rate of glycolysis
3. The rate of K⁺ leaving the cell through a potassium channel is a major determinant of the polarization of the cell membrane
4. ATP inhibits the K⁺-channel, the more ATP, the less K⁺ leaving the cell, and the less polarized (more depolarized) the cell membrane
5. Depolarization causes Ca⁺⁺ to exit the cell and insulin leaves the cell through the insulin transporter

All of the following statements about the pentose phosphate pathway are true EXCEPT

1. Its two functions are to produce NADPH and ribose-5-P
2. It uses glucose-6-P as a substrate when producing NADPH and CO₂
3. Glucose-6-phosphate dehydrogenase is the control enzyme and it is regulated by the NADPH concentration of the cell
4. If it is producing more than twice as much NADPH as ribose-5-P, it can produce glyceraldehyde-3-P and fructose-6-P
5. It is found in the mitochondria of liver, muscle and brain but is absent from most other tissues of the body

Your patient has a high serum homocysteine level and a defect in the enzyme that transfers one-carbon units from N⁵-methyltetrahydrofolate to form methylcobalamin (B₁₂).  The greatest change from normal would be in the rate of conversion of

1. Methionine to homocysteine
2. Homocysteine to methionine
3. Homocysteine to succinyl CoA
4. Serine to cysteine
5. Cysteine to pyruvate and H₂SO₄

Correct answers and percentage of the class answering correctly. As a reference point, it is estimated that previous classes would have scored a combined mean of 68.3% for questions 1 through 93.

1, D, 76%, Chapter 4, Objective 3: "Define pH. Given any hydrogen ion concentration, determine the pH and visa versa."

2, E, 86%, Chapter 4, Objective 12: "Draw the dissociation of ammonium ion. If the pKa =9.3, what form is found at pH =7?"

3: D, 80%, Chapter 4, Objectives 7 and 12: "Given a weak acid, be able to draw the equation for its dissociation and label the conjugate base (salt of the acid). Be able to define the Ka for the acid. Be able to write the Henderson-Hasselbalch equation for acid. Draw the dissociation of ammonium ion. If the pKa =9.3, what form is found at pH=7?"

4: B, 60%. Chapter 4, Objective 14: "Regarding the Di Beatty Case: Explain why an increase in a metabolic acid would cause the changes seen in PaCO₂ and serum bicarbonate. What would happen to the concentration of CO₂ and serum bicarbonate after the insulin injection?"

5: D, 44%. Chapter 5, Objective 16: "What does the lyso in lysolecithin indicate?"

6. A, 67%, Chapter 5, Objectives 14, Recognize a mono, di and triacylglycerol

7: A, 69%. Chapter 6, Objective 13: " Given any amino acid except cysteine serine, threonine and tyrosine, be able to predict the isoelectric point!"

8. A, 31%, Chapters 6, Objectives 1 and 10: "What is the approximate pKa for all alpha-amino groups and for all alpha-carboxyl groups? Are they charged at pH=7? Given the pH, predict whether the amino acids aspartic acid, glutamic acid histidine, lysine, and arginine would be neutral or would carry a net negative or net positive charge."

9: B, 70% Chapter 6, Objective 10:" Given the pH, predict whether the R-groups of the amino acids aspartic acid, glutamic acid, histidine, lysine, and arginine would be neutral or would carry a net negative or net positive charge".

10: C, 54%. Chapter 6, Objective 10: "Given the pH, predict whether the amino acids aspartic acid, glutamic acid, histidine, lysine, and arginine would be neutral or would carry a net negative or net positive charge."

11: D, 72%. Chapter 7, Objective 7: "What is a structural domain?"

12: C, 55%. Chapter 7, Objective 26: " Concerning Amy Lloyd: What is an amyloid protein? What are the monomer units of the polymer in amyloidosis/AL? What secondary structure is found in amyloid fibers? What is an M-protein and why is it detected as a sharp peak upon serum protein electrophoresis?"

13: E, 66%. Chapter 7, Objective 24: " Concerning Will Sichel: In biochemical terms, explain the development of pain during a sickle cell crises. Include the specific mutation, oxygen pressure, and protein conformation in your answer.."

14. D, 64%, Chapter 7, Objective 2 "Be able to recognize and discern between the three types of secondary structure discussed in class!."

15. E, 43%, Chapter 7, Objective 27 " Concerning Di Abietes, What is HbA_1c? How is it made and what does it measure?"

16. D, 81%, Chapter 7, Objective 24 " Concerning Will Sichel: In biochemical terms, explain the development of pain during a sickle cell crises. Include the specific mutation, oxygen pressure, and protein conformation in your answer."

17: E, 47%. Chapter 8, Objective 12: "Concerning NAD⁺, what vitamin is it synthesized from? When lactate dehydrogenase or alcohol dehydrogenase oxidize their substrates, what is transferred to NAD⁺? Besides pyruvate and acetaldehyde, what is the other reaction product? What is the function of the ADP portion of NAD⁺?"

18: E, 18%. Chapter 8, Objective 18: "Explain why allopurinol is used to treat gout. Is allopurinol a irreversible inhibitor? Is allopurinol a suicide inhibitor? Why?"

19. B, 81%, Chapter 8, Objective 5: "Define catalytic power. Explain catalytic power in terms of the transition state and activation energy."

20: A, 83%. Chapter 9, Objective 16: "Explain how an increase in calcium in muscle cells simultaneously activates muscle contraction and glycogenolysis. Which system uses ATP and which helps to produce ATP?"

21: D, 70%, Chapter 9; Objective 4, " What is the effect of a competitive inhibitor on the K_M and V_max?"

22: E, 35%. Chapter 9, Objectives 8 :"The substrates of allosteric enzymes exhibit positive cooperativity. Explain positive cooperativity in terms of conformation and activity of the active site."

23: A, 50%, Chapter 11, Objectives 9 and 10, " When a protein contains a src homology 2 domain (SH2 domain), what does it bind to? Is the binding specific? " " In the Ras and MAP kinase pathway, how does the occupied receptor activate Grb2? What is the last step in the pathway that is catalyzed by MAP-kinase and what is the effect?"

24: C, 62%, Chapter 11, Objectives 11 and 25, " What are the functions served by phosphatidylinositol phosphates in signal transduction? " " When phosphatidyl inositol bisphosphate is hydrolyzed by phospholipase C, what is the next step in the signal transduction pathway for diacylglycerol? What are the next several steps in the signal transduction pathway for inositol trisphosphate? Use protein kinase C, target proteins, endoplasmic reticulum, calcium, calmodulin, and calmodulin binding proteins in your answer."

25: E, 70%, Chapter 11, Objectives 3 and 27, " Beginning with the response to a stimulus, list the common characteristics of all chemical messenger systems as they apply to the chemical messenger acetylcholine at the neuromuscular junction. Use the terms nerve cell action potential, Ca2+-channel, vesicles, fusion, presynaptic membrane, acetylcholine, diffusion, acetylcholine receptors, gated ion channels, muscle cell action potential, and acetylcholinesterase." " Concerning Mya Sthenia who has myasthenia gravis, explain how her chemical messenger system differs from a normal person. How did this happen? Why do the anticholinesterase drugs do to temporarily alleviate the problem?"

26: E, 83%. Chapter 19, Objective 8: "Given two equations with the Delta G^o' for each reaction, be able to add or subtract an equation and determine if the reaction as spontaneous."

27: A, 85%. Chapter 19, Objective 16: "How do NAD, FAD, and FMN function?"

28: E, 68%. Chapter 19, Objective 20: "Assume a sudden loss of oxygen supply to a cell. Give a simple scenario (sequence of events) that might lead to cell death (necrosis) and release of enzymes. Use the terms hypoxia, oxidative phosphorylation, ATP concentration, active transport, intracellular Ca²⁺, swelling, permeability, and creatine kinase."

29: D, 22%, Chapter 19, Objective 9: "Given the equation at the bottom of Table 19.2, be able to explain why delta-G can be positive while delta-G^o' is negative and vice versa."

30: B, 32%. Chapter 19, Objective 13: "Be able to describe how the hydrocarbons in our diet are converted to CO₂, H₂0, and ATP. Include the reduction and oxidation of coenzymes and the creation and use of proton gradients in your explanation."

31: E, 98%. Chapter 19, Objective 17 :" What is an anaerobic pathway? What is anaerobic glycolysis?"

32: A, 72%. Chapter 20, Objective 8: "Name the five cofactors of the a-ketoglutarate dehydrogenase reaction. Name the vitamins from which four of them are derived! What is the advantage of a multienzyme complex?"

33: E, 76%. Chapter 20, Objectives 11 : "How is the rate of the TCA cycle linked to muscle contraction and the utilization of ATP?"

34: B, 86%. Chapter 20, Objective 1: "To describe any pathway or cycle, start with the following paradigm for the TCA cycle: Names: Functions: Substrates: Products: Control Enzymes: Regulation: Compartment: Tissues of Interest:"

35. C, 58%, Chapter 20, Objective 2: "Name the four dehydrogenase enzymes of the TCA cycle. What are the substrates and products of each reaction?"

36. D, 81%, Chapter 20, Objectives 16 and 17: "Explain how the rate of the pyruvate dehydrogenase complex is related to the rate of utilization of ATP" " Explain how muscle contraction is related to the rate of the pyruvate dehydrogenase reaction."

37: C, 74%. Chapter 20, Objective 29:"Concerning Al Martini: Given that a-ketoacids build up in the heart in wet beriberi, develop a scenario that would explain why peripheral vessels dilate and cardiac muscles loose their contractility."

38: E, 71%. Chapter 21, Objective 15: "Be able to go through the series of events whereby pyruvate dehydrogenase is activated by increased ATP utilization."

39: E, 68%. Chapter 21, Objective 11: "What portion of the ETC is inhibited by CN^-? What is the effect of cyanide inhibition upon proton pumping and ATP synthesis?"

40. B, 64%, Chapter 21, Objective 8: "Be able to state the chemiosmotic theory!"

41. C, 45%, Chapter 21, Objective 17: "What is the difference between an inhibitor of electron transport and an uncoupler of electron transport with respect to NADH utilization, proton pumping, and ATP synthase?"

42: A, 64%. Chapter 21, Objective 22: "Concerning X.S.Teefore, Explain how the affect of excess thyroid hormone on oxidative phosphorylation could explain increased appetite and sweating?"

43: E, 67%. Chapter 21, Objective 16 and 17:" Understand how a chemical uncoupler works. What happens to heat production, proton pumping, ATP synthesis, and NADH utilization following uncoupling?" "What is the difference between an inhibitor of electron transport and an uncoupler of electron transport with respect to NADH utilization, proton pumping, and ATP synthase?"

44: D, 30%. Chapter 22, Objective 11: "Compare the energy produced from glucose during anaerobic glycolysis with the energy produced in the conversion of glucose to pyruvate during aerobic glycolysis. How much energy is produced if glucose is completely oxidized to CO₂?"

45: E, 81%. Chapter 22, Objective 22: "Concerning Otto Shape, compare his metabolism when walking slowly with sprinting. Consider the following: Total ATP used by muscle per second. Rate of ATP generated by oxidative phosphorylation. The rate of pyruvate oxidized by pyruvate dehydrogenase and the TCA cycle. Why?. The rate of glycolysis. Why?. The rate of conversion of pyruvate to lactate. Why?"

46: A, 55%, Chapter 22, Objective 14: "Explain the Cori cycle."

47: B, 90%. Chapter 22, Objectives 21:"Concerning Lopa Pusor: Explain why hemorrhage, anemia, COPD, or any combination of these three might result in lactic acidosis"

48: E, 38%. Chapter 23, Objective 4: "What are the reactants and products of the fatty acyl CoA synthetase reaction?"

49: E, 80%. Chapter23, Objective 10: " Describe the pathway for the synthesis of ketone bodies by naming substrates, the first ketone body made in the pathway, the next two ketone bodies made in the pathway, the intermediate in the pathway that can be used either for ketone body synthesis or cholesterol synthesis, and the enzyme that actually produces the first ketone body as a product. Control? Where does this pathway reside?"

50: C, 95%, Chapter 23, Objective 2: "How are free fatty acids transported from adipose tissue to muscle or liver cells?"

51: C, 65% Chapter 23, Objectives 8 and 10: " Be able to name the three metabolites and two important cofactors in the conversion of part of an odd chain fatty acid to a TCA cycle intermediate. (Skip the epimerase) reaction.)" "Describe the pathway for the synthesis of ketone bodies by naming substrates, the first ketone body made in the pathway, the next two ketone bodies made in the pathway, the intermediate in the pathway that can be used either for ketone body synthesis or cholesterol synthesis, and the enzyme that actually produces the first ketone body as a product. Control? Where does this pathway reside?"

52: B, 63%. Chapter 26, Objective 6: "What is the effect of glucagon upon the following metabolic pathways...the storage of glucose in glycogen, the mobilization of glucose from glycogen, the synthesis of fatty acids from glucose in the liver, the synthesis of triacylglycerols in liver and adipose tissue, the mobilization of free fatty acids from adipose tissue, and the mobilization of amino acids from proteins for gluconeogenesis."

53: C, 46%. Chapter 26, Objective 26: "Concerning Bea Selmass...Explain why a patient with an insulinoma would have fasting hypoglycemia."

54. E, 37%, Chapter 26, Objective 20: "Concerning Ann Sulin: She has type 2 and her blood insulin levels are within the normal range. Are her B-cells secreting enough insulin? Are her muscle and adipose cells responding normally to insulin?"

55: D, 92%. Chapter 26, Objective 9:"Know the important events in the synthesis of insulin from synthesis of the preprohormone to precipitation in storage granules".

56: D, 79%. Chapter 28, Objective 20: "Concerning Jim Bodie...Jim injected insulin just before exercise. What were the affects upon the pathways and transport mechanisms of the liver and muscle that led to his hypoglycemic coma?"

57: C, 83%, Chapter 28, Objectives 5 and 11: "Describe the pathway for glycogen synthesis from glucose in liver and muscle: Name, Function, Substrates, Products, Control Enzyme, Regulation, Compartment. What is the effect of changes in the insulin, blood glucose or epinephrine upon glycogen synthesis or glycogen degradation in muscle?"

58: D, 81%. Chapter 28, Objective 2:"What are the functions of glycogen in liver and skeletal muscle? Why must glucose-6-phosphate produced from glycogen in muscle enter glycolysis? Why does glucose produced from glycogen in liver usually enter the blood stream instead of glycolysis?"

59: D, 81%. Chapter 28, Objective12: " In order of their activation, be able to name and give the reason for the activation of all the intermediates in the cAMP cascade in liver. Start with a decrease in the insulin/glucagon ratio or an increase in epinephrine and end with the change in activity of glycogen synthase, phosphorylase kinase and phosphorylase a?"

60: D, 82%. Chapter 31, Objective 7: " Describe the pathway for the conversion of pyruvate to phosphoenolpyruvate by naming the intermediates, the compartments, the control enzyme, and the allosteric regulator for the control enzyme. Include the terms pyruvate carboxylase, biotin, ATP, oxaloacetate, acetyl CoA, malate dehydrogenase, NADH, malate, phosphoenolpyruvate carboxykinase, GTP. Ignore aspartate"

61: D, 80%, Chapter 31, Objective 12: "Name the enzyme that converts glucose-6-phosphate to glucose in liver."

62. C, 78%, Chapter 31, Objective 3: "What are the sources of the gluconeogenic precursors and how are they converted into pyruvate, TCA cycle intermediates, or dihydroxyacetonephosphate?"

63: D, 87%. Chapter 29, Objective 1: "Describe the pentose phosphate pathway ...Names, Functions, Substrates, Product, Control Enzymes, Regulation, Compartment(s), Tissues of interest."

64: D, 82%, Chapter 29 Objective 3: "What is NADPH used for?"

65: C, 56%, Chapter 29, Objective 5: "Concerning Al Martini: This patient has glucose-6-phosphate dehydrogenase deficiency. Why are red blood cells lysed while other cells of the body remain intact? Why didn't this disease show up earlier in life?"

66: E, 80%. Chapter 31, Objective 25: " Be able to state the major source of glucose (ingested, glycogenolysis, or gluconeogenesis) used by a sedentary person following ingestion of a meal. For example, at l hour, 4 hours, 16 hours, and 30 hours. Assume that the subject was sedentary. What would happen to this timetable if the person were running a marathon?"

67: C, 88%. Chapter 31, Objective 24: "Between 3 days and 6 weeks of starvation, what happens to the blood concentrations of glucose, free fatty acids, and ketone bodies? What happens to the total utilization of glucose by the body? What happens to the total utilization of fat by the body? Between 3 days and 6 weeks of starvation, what happens to total urinary nitrogen excretion? Note that total urinary nitrogen is at least 80% urea. Explain this change in urea excretion."

68. D, 79%, Chapter 31, Objective 25: " Be able to state the major source of glucose (ingested, glycogenolysis, or gluconeogenesis) used by a sedentary person following ingestion of a meal. For example, at l hour, 4 hours, 16 hours, and 30 hours. Assume that the subject was sedentary. What would happen to this timetable if the person were running a marathon?"

69: A, 90%, Chapter 33, Objective 8: "What are the essential fatty acids and why are they essential?"

70: C, 90%. Chapter 33, Objective 16:"In the synthesis of membrane lipids, what is the function of SAM?"

71: A, 56%. Chapter 33, Objective 6:" Where does the elongation of most fatty acids take place?"

72: E, 60%. Chapter 33, Objective 19: " Concerning Colleen Lakker: What was the cause of respiratory distress syndrome of this premature infant? What specific compounds are missing? Are any derivatives of phosphatidic acid?"

73: E, 82%. Chapter 36, Objective 1: " Describe the pathway for the storage of glucose in the liver in the fed state? How is this pathway regulated.? Are there any possible futile cycles prevented?"

74: E, 60%. Chapter 36, Objective 20: "Concerning Di Beatty who has type I diabetes has developed ketoacidosis...On a molecular level, explain why she has opalescent serum. Why does she have high blood glucose? Why does she have ketonemia?"

75: D, 77%, Chapter 36, Objective 20: "Concerning Di Beatty who has type I diabetes has developed ketoacidosis...On a molecular level, explain why she has opalescent serum. Why does she have high blood glucose? Why does she have ketonemia?"

76: B, 86%. Chapter 36, Objective 15:" What is the control enzyme for the release of free fatty acids during a fast and how is this enzyme regulated?"

77: C, 96%. Chapter 38, Objective 5:"What are the cofactors for ALT and AST. Are the coenzymes prosthetic groups? What vitamin are the cofactors derived from?"

78: E, 43%. Chapter 38, Objective 18: "Concerning Percy Veere who has hepatitis A: Why would a low protein diet, antibiotics, enemas and lactulose lower his blood ammonium ion level?"

79: C, 89%. Chapter 38, Objective 12: "Know the substrates, products, and five enzymes of the urea cycle. Which compartments are involved? What tissues are involved?"

80: B, 56%, chapter 38, Objective 4: "Be able to write a reaction for AST, ALT, or any other transamination reaction. What is the approximate Keq for these reactions?"

81: C, 79%. Chapter 39, Objective 1: "What is an essential amino acid? Which ones are they?"

82: E, 71%. Chapter 39, Objective 13: " Concerning Homer Sistine: If he had an inborn error in cystathionine synthase, what would happen to his concentrations of methionine, homocysteine, and cysteine? Why? If his problem had been a deficiency of folate or vitamin B₁₂ , what would you expect to happen to the concentrations of methionine, homocysteine, and cysteine? Why?"

83. C, 76%, Chapter 39, Objective 5: "For each amino acid, be able to say where its catabolic products enter the TCA cycle, the glycolytic/gluconeogenic pathways, or the ketone body pathway."

84. A, 58%, Chapter 39, Objective 13: " Concerning Homer Sistine: If he had an inborn error in cystathionine synthase, what would happen to his concentrations of methionine, homocysteine, and cysteine? Why? If his problem had been a deficiency of folate or vitamin B₁₂ , what would you expect to happen to the concentrations of methionine, homocysteine, and cysteine? Why?"

85: D, Estimated 70%, Chapter 4, Objective 14: Regarding the Di Beatty Case: Explain why an increase in a metabolic acid would cause the changes seen in PaCO₂ and serum bicarbonate. What would happen to the concentration of CO2 and serum bicarbonate after the insulin injection?

86: B, Estimated 70%, Chapter 6, Objective 16: Concerning Michael Sichel: To the extent covered in this chapter, explain his disease in terms of amino acids. In the African American population, is the Sickle Cell allele a polymorphism?

87: D, Estimated 70%, Chapter 8, Objective 21: Be able to name the 6 major classes of enzymes. Given one of the following reactions, be able to match it with one of the 6 major classes of enzyme reactions catalyzed: alcohol dehydrogenase, glucokinase, chymotrypsin, aldolases, triosephosphate isomerase, and pyruvate carboxylase.

88: B, Estimated 70%, Chapter 8, Objective 24: Name the enzyme that synthesizes cAMP, the enzyme that hydrolyses cAMP and the enzyme that is activated allosterically by cAMP. Which of these three enzyme reactions is affected by insulin?

89: E, Estimated 70%, Chapter 20, Objective 29: Concerning Al Martini: Given that a-ketoacids build up in the heart in wet beriberi, develop a scenario that would explain why peripheral vessels dilate and cardiac muscles loose their contractility.

90: D, Estimated 70%, Chapter 22, Objective 19: In cardiac muscle, high adrenalin and high cAMP will activate protein kinase A. High protein kinase A activity will phosphorylate the enzyme phosphofructokinase-2/fructose-2,6-bisphospahtase. How will this effect the activity of phosphofructokinase 1 and the rate of glycolysis?

91: E, Estimated 70%, Chapter 26, Objective 10: Describe the mechanism of release of insulin from beta cells in response to increased blood glucose. Include the terms: blood glucose, glucose transporter, glucokinase, glycolysis, ATP concentration, ATP sensitive K⁺ channel, membrane depolarization, calcium concentration, exocytotic vesicle, plasma membrane, fusion, insulin release

92: E, Estimated 70%, Chapter 29, Objective 1: Describe the pentose phosphate pathway; Names: Functions: Substrates: Product: Control Enzymes: Regulation: Compartment(s): Tissues of interest

93: B, Estimated 70%, Chapter 39, Objective 13: Concerning Homer Sistine: If he had an inborn error in cystathionine synthase, what would happen to his concentrations of methionine, homocysteine, and cysteine? Why? If his problem had been a deficiency of folate or vitamin B₁₂ , what would you expect to happen to the concentrations of methionine, homocysteine, and cysteine? Why?