1. Draw the Fisher projection of D-glucose, and from Fisher to Haworth projection of ẞ-D-glucose. Label (R) and (S) configuration for each chiral carbon Fisher projection Haworth projection
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- 4 A I. Refer to the figure below and answer the following questions: 45 5 55 6 65 PH 7 75 8.5 0 10 B 15 20 25 30 35 Temperature (°C) 40 45 Legend: Blue - wild-type ß-galactosidase; Red - mutant ß-galactosidase a. What is the optimum pH of wild type ß-galactosidase? b. What is the optimum temperature of mutant ß-galactosidase? c. Which enzyme has the greater activity at pH 7.2? d. Which enzyme has the greater activity at a temperature of 42.5°C? e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? f. Which enzyme has greater activity if temperature increases from 40°C to 41 °C? 50 55ALANINE AMINOTRANSFIRASE AND ASPARTATE AMINOTRANSFERASE (KARMEN МЕТHOD) (C. chemistry) 1. state the reason why substrate must be incubated prior to the addition of serum 2. what part of the steps need extra to avoid positive results? 3. describe the principle of AST/ALT kinetic method.3. (a) The activity of the Pentose Phosphate Pathway is commonly quantified by measuring 14CO2 production from C-14 labeled glucose. In this assay, glucose is metabolized aerobically by cells or tissue slices; both [1-14C] glucose and [6-14C] glucose are employed separately but in parallel. This classical method, thus, requires two separate assay mixtures. Which radioactive isotopomer of glu- cose releases 14 CO2 generated by the Pentose Phosphate Pathway? Confirm your conclusion by drawing the intermediates of the oxidative phase of the PPP with structural formulas, starting with glucose-6-phosphate. Name the intermediates and indicate enzymes. (b) ( Because the assay protocol requires aerobic incubation of cells or tis- sue slices with isotopically labeled glucose in parallel assays, what is the purpose of the other radioactive glucose derivative? To answer this question base your answer using the diagram on the right. O2 NADH CH₂OH + 2 NAD+ HO HO + 2 Pj 2 CO + 2 ATP HO OH 2 ADP CH3…
- 3. (a) The activity of the Pentose Phosphate Pathway is commonly quantified by measuring 14CO2 production from C-14 labeled glucose. In this assay, glucose is metabolized aerobically by cells or tissue slices; both [1-14C] glucose and [6-14C] glucose are employed separately but in parallel. This classical method, thus, requires two separate assay mixtures. Which radioactive isotopomer of glu- cose releases 14 CO2 generated by the Pentose Phosphate Pathway? Confirm your conclusion by drawing the intermediates of the oxidative phase of the PPP with structural formulas, starting with glucose-6-phosphate. Name the intermediates and indicate enzymes. (b) ( Because the assay protocol requires aerobic incubation of cells or tis- sue slices with isotopically labeled glucose in parallel assays, what is the purpose of the other radioactive glucose derivative? To answer this question base your answer using the diagram on the right. O + 2 NADH CH₂OH + 2 NAD+ ○ HO HO + 2 Pi 2 CO + 2 ATP HO OH 2 ADP…what is lactose intolerance ? describe the molecular life cycle for this disease. also describe how it occurs in a molecular level detailed mechanism. what causes this disease and how it develops ? provide detailed biochemical phenomena and life cycle for Lactose Intolerance condition.25. Overall oxidation of glucose can be represented as (2 Points) Glucose + 2ADP + 2GDP + 4 Pi +8NAD+ + 2FAD + 2H2O-----> 6CO2 + 2ATP + 2GTP +8NADH + 6H+ + 2FADH2 Glucose + 4ADP + 2GDP + 4 Pi +8NAP+ + 2FAD + 2H2O-----> 6CO2 + 2ATP +2GTP +8NADH + 6H+ + 2FADH2 Glucose + 2ADP + 2GDP + 4 Pi +8NADP+ + 2FAD + 2H2O-----> 2CO2 + 2ATP + 2GTP +8NADHP + 6H+ + 2FADH2 Glucose + 2ADP + 2GDP + 2 Pi +6NAD+ + 2FAD + 2H2O-----> 6CO2 + 2ATP + 2GTP +6NADH + 6H+ + 2FADH2
- 1. The human hemoglobin molecule, like all mammalian he- moglobins, is comprised of two a-chains and two ß-chains con- ₂ taining 141 and 146 amino acid residues, respectively. Be- cause the molecule possesses two-fold symmetry, there are a1-a2, B1-B2, and a1-B2 interfaces formed by amino acid sidechains through which structural changes are transmitted underlying ligand binding. The most important of these is the a1-B2 interface that is illustrated in the diagram on the right. All of the sidechain interactions across the a1-B2 interface are hydrophobic except for that between Asp(a94) and Asn- (B102). This is the only polar interaction across the α1-³2 in- terface and it helps to stabilize the oxy- or R-conformation. Its approximate location in the Hb molecule is represented by the red double arrow in the diagram on the right. His FG4 97 Asp G1 (99) Tyr C7 (42) Hb mutant (a) T State (deoxy) 95 The C6 41 (a) The diagram below on the right-hand side illustrates the polar Asp(a94). . . Asn…16. The overall reaction for the glycolysis reaction is C6H₁2O6(aq) + 2NAD+ (aq) + 2ADP³(aq) + 2HPO(aq) + 2H₂O(1) 2CH3COCO₂ (aq) + 2NADH(aq) + 2ATP4 (aq) + 2H3O+ (aq). What is A,G at chemical equilibrium?. Provide an explanation for the fact that a-D-mannose is more stable than B-D-mannose, whereas the opposite is true for glucose.
- 6. A. List all of the ionizable functional groups that are found in insulin when in aqueous solution. List which amino acid residues have these ionizable groups and list all of the pka and pKb values (including the R groups) that are on both polypeptide chains that make up insulin. (see the table at the end of this HW set; note that tyrosine and cysteine both have unusual pka's, since these side groups ionize above the pKR's given to have a negative charge). B. The isoelectric point of insulin is reported to be around 5.3-5.35. Using the method covered in class, estimate the isoelectric point of insulin and compare your answer to the values above. C. For a polypeptide to be soluble in an aqueous solution, is it good to be near the isoelectric point? Why or why not? Notes: a couple of unusual R group's that ionize (cysteine and tyrosine have R groups that have pka values; histidine has a pkb). The table at the end of this homework set (also in the lecture notes) lists the pka's and…2. The two diagrams to the right il- lustrate plots of steady-state ki- netic studies to characterize the in- FB 0.8- nH = 3.5 0.6- teraction of heart muscle phos- phofructokinase-1 with a non-phy- siological, synthetic substrate fruc- tose-6-sulfate. Because the kcat is smaller than that for the natural 0.4- 0.2- 10 μΜ 20 μΜ 48 μΜ substrate, higher enzyme concen- trations could be used. The results show the influence of increasing 2- 3.2- 0.4- concentrations of ATP on the initial -0.6- > velocity of the enzyme catalyzed reaction in the presence of no AMP (•), 10 µM AMP (•), 20 µM AMP (-), and 48 µM AMP (-). -0.8- 4 12 20 28 36 44 52 60 68 76 84 92 1.2 1.6 2.0 2.4 [AΤP (μΜ) log[ATP] (µM) (a) how ATP interacts with the enzyme in the case of no AMP (•). Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe (b) with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme. Explain the physical significance of the…what are the molecular way to diagnose Lactose intolerance disorder ? describe in detail about diagnostic phenomena of lactose intolerance and possible treatment.
