1. Draw and label completely the electrophoretic pattern of CK isoenzymes 2. What are the sources of error in Amylase determination?
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1. Draw and label completely the electrophoretic pattern of CK isoenzymes
2. What are the sources of error in Amylase determination?
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- 5. (a) Hexokinase IV is known as glucokinase (GCK) and is a central metabolic enzyme that participates in glucose homeostatic maintenance by governing the rates of glucose catabolism in pan- creatic B-cells and glycogen storage in hepatocytes (liver cells). In contrast to the regulatory mecha- nisms of hexokinase I or Il in other tissues, GCk is regulated by binding to the Glucokinase Regulatory Protein (GRP) located in the cell nucleus. When glucose in hepatocytes is low, GCK is sequestered in the nucleus by binding to the GRP. High glucose, for instance, after ingestion of a meal, disrupts the GRP-GCK complex, allowing the GCK to diffuse into the cytoplasm to convert glucose into glucose-6- phosphate. Contrast the properties of hexokinases I and IV with respect to oligomeric structure, mech- anism of regulation of their activity, KM value, and dependence of catalytic activity on cellular location. Hexokinase l is found in, for instance, muscle tissue. Property subunit structutre…2. In contrast to the toxicity of 2-fluoro-citrate, L-(2-fluoro-)succinate is not an inhibitor of succinate dehydrogenase and the product 2-fluoro-fumarate is converted by fumarate hydratase to L-(2-fluoro-2- hydroxy)malate that breaks down to oxaloacetate. (a) the FAD coenzyme of succinate dehydrogenase as the normal substrate? Write the reaction with structural formulas to illustrate your answer. Does the oxidation of 2-fluoro-succinate yield the same number of reducing equivalents to (b) droxy)malate, which breaks down spontaneously to oxaloacetate. Write the equation with structural formulas. 2-fluoro-fumarate is a substrate of fumarate hydratase forming only L-(2-fluoro-2-hy- Oxaloacetate has been shown to be a very po- (c) tent inhibitor of succinate dehydrogenase. For the enzyme 3 isolated from cardiac muscle the Kj value is ~4 x 10-6M, as shown in the L-B plot on the right. Yet, this inhibition is never discussed in biochemistry textbooks. From your reading in the textbook,…5. pertaining to glycolysis, gluconeogenesis, TCA cycle, glycogen breakdown and synthesis
- 2. Below is experimental data regarding mode of inhibition of "“Enzyme K" by sucralose. This is a double- reciprocal plot of enzyme velocity (Vo) versus substrate concentration, and each line represents a series of data collected at a different sucralose concentration. This is preliminary experimental data, so for a first- approximation of the experimental data, velocity data without inhibitor present can be overlooked (ignored). 0.04 00 mM sucralose 0.035 O 2.5 mM sucralose 0.03 O 10 mM sucralose 0.025 0.02 0.015 0.01 0.005 -6 2 4 -0.005 -0.01 1/ [substrate] (mM) A) Propose a mechanism of inhibition of this enzyme by sucralose. B) Explain your reasoning to part A). 1/V. (mM1 min)1.A blood test returns elevated aspartate aminotransferase levels. You suspect that the patient has suffered a heart attack. What other serum enzyme level of the ones listed should be tested to confirm the diagnosis? A.acid phosphatase B.lysozyme C.amylase D.alkaline phosphatase E.creatine kinase 2.A blood test returns elevated acid phosphatase levels. What disease(s) is indicated by this test result? select all that apply A.mumps B.bone disease C.prostate cancer D.heart attack E.hepatitis3. In your textbook the termi- nal enzyme catalyzing the ter- minal step of glycolysis is known as pyruvate kinase (PK). No indication is given that in mammalian tissues there are four different iso- forms of this enzyme. The four mammalian isoforms are known as PKL, PKR, PKM1 and PKM2. PKL is expressed in the liver, and PKR is ex- pressed in red blood cells. C PKM1 and PKM2 are derived from altemative splicing of the PKM gene. PKM1 is a constitu- tively active isoform expressed Active Site A PKM2 Monomer B Fructose-1,6-Bisphosphate N Phe, Ala, Ser Binding Site PKM2 Tetramer "Activator" Binding Site in differentiated cells from various tissues. In contrast, PKM2 has low basal activity and is activated by an effector molecule fructose 1,6-bisphosphate (FBP). PKM2 is expressed in most proliferating cells. In addition, the regulation of PKM2 pyruvate kinase activity plays an essential role in cancer metabolism and is crucial for the growth and survival of cancer cells. Recently, PKM2 has…
- 6. When a concentrated alkali solution acts on the purine cycle, it breaks down: A. Ester group B. Imidazole nucleus C. Dioxopyrimidine nucleus D. Lactone cycle 7. According to the Pharmacopoeia, sodium thiopental is quantitatively determined by the following methods: A. Acidimetry B. Alkaimetry C. Gravimetry D. HPLC E. UV spectroscopy 8. When determining the content of free alkali in sodium salts of barbiturates, an indicator is used: A. Methyl orange B. Methyl red C. Timolphthalein D. Phenolphthalein 9. NH-acidic properties are shown by: A. Sulfacyl sodium B. Sodium barbital C. Theobromine D. Hexamidine (primidone) 10. Derivatives of pyrimidine-2,4-dione are derivatives: A. Uracil B. Uretane C. Barbituric acid D. Malonic acid 11. The cerimetric method can be used for quantitative analysis: A. Nicotinic acid B. Atropine sulfate C. Gomatropin hydrobromide D. Nicotinic acid diethylamide E. NifedipinPlease give me detailed information and explain.1. The Fehling’s reaction, which is a simple assay for reducing sugars, was used as a diagnostic test for the determination of blood glucose concentrations for a very long time. However, it has now been replaced by the glucose oxidase test. The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone. This enzyme is highly specific for the β-anomer of glucose and does not affect the α-anomer. In spite of this specificity, the reaction catalyzed by glucose oxidase is commonly used in a clinical assay for total blood glucose—that is, for solutions consisting of a mixture of β- and α-D-glucose. Explain how this is possible. Aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over Fehling’s reagent for the determination of blood glucose? 2. Consider only the oxygen levels present in the cytoplasm and ECF as shown in the drawing above (no new oxygen is entering…
- 3. Acetylcholinesterase is a serine hydrolase enzyme im- portant in nerve signal transmission, hydrolyzing acetylcho- line, an ester molecule with a positively charged quaternary nitrogen group. The structure of the physiologically relevant substrate of this enzyme is shown on the right. The quater- H₂C nary nitrogen group serves to anchor the molecule in the active site Gly121 Oxy- anion hole Gly122 Ala204 Substrate ACh His447 Catalytic triad Ser203 Glu202 Glu334 Ser229 CH3 N+ CH3 CH3 The a Scale document down rine protease family, consisting of a catalytic triad Ser203- His447-Glu334 with Ser203 supplying the nucleophilic hydroxyl group and an oxyanion hole com- prised of peptide NH groups of Gly121, Gly122, and Ala204, illustrated in the diagram above, for which carbon (green), nitrogen (blue), and oxygen (red) atoms are shown while hydrogen atoms are white. The enzyme catalyzed reaction can be represented by the following scheme: (a)( k1 K2 E + S = ES K-1 K3 EYE + P where ES…1. How would ATP production in an aerobic yeast culture change if we add the following metabolites or chemicals to the cultivation media? Explain why in each case by citing which enzyme(s) or process(es) would be affected.6. Provide a biochemical explanation for the fact that some patients with homocystinuria respond to vitamin Bo, while others do not. 7. In addition to the reaction shown in the metabolic pathway, vitamin Bo participates in a considerable number of other metabolic reactions of amino acids. Why does the daily requirement for vitamin Be vary according to the amount of protein in the diet? 1.