HbF HbA + 2.5 mM BPG 1.0 Given the oxygen dissociation curves, which of the HbA, HbF + following statements are correct? 2.5 mM BPG 0.8 HbA lysate O Purified HbA has a higher oxygen affinity than purified HbF. 0.6 2,3-BPG is an allosteric activator of HbA. The allosteric effects of 2,3-BPG are homotropic. 0.4 2,3-BPG only weakly interacts with HbF. HbF loads oxygen at lower pO, than does HbA in the 0.2 presence of 2,3-BPG.
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Given the oxygen dissociation curves, which of the following statements are correct?
Which residue in HbA β do you think contributes the most to the increased interaction between HbA aand 2,3‑BPG?
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- TABLE 3-LACTATE PRODUCTION IN FORTIFIED HEMOLYSATES OF HUMAN ERYTHROCYTES* Substrate Glucose Glucose Lactate production† No. of experiments pH 6 7.1 2.03 ± 0.91 6 7.8 4.76 ± 1.09 7-1 10-73 +1-88 5 7.8 12.34 ±2.92 5 7.0 7-15±0.73 5 7-7 (b)( ) In mature erythrocytes (red blood cells) the end product of glycolysis is lactate because of the absence of mitochondria. On the right is a table comparing the rate of lac- tate production in hemolysates (lysed cells) of human RBCs as a function of pH with dif- ferent substrates introduced into the glyco- lytic pathway. The hemolysate was fortified with 30 μmoles substrate, 7.5 μmoles MgCl2, 10 μmoles disodium phosphate, 1.5 μmoles NAD and 5 μmoles ATP in a volume of 5 mL. The rate of lactate production is given as μmoles of lactate/g Hb/hr at 37° C, buffered to either pH 7.1 or 7.8, as indicated. According to the results in the table which glycolytic enzyme is rate-limiting? Explain. Glucose-6-phosphate Glucose-6-phosphate Fructose-1,6-diphosphate…1.1 ;) The diagram on the right compares the O2 binding prop- 1.0 erties or normal adult hemoglobin (HbA) to those of one dubbed Hb Great-Lakes characterized by the mutation Leu(B68)His. In the dia- gram Y = fraction of heme groups with bound O2, and pO2, the par- tial pressure of O2 above the solution, is measured in units of torr or mmHg. Hb Great Lakes %3D 0.8 Hb A 0.6 Draw the corresponding Hill plot, being careful to reproduce graph- ically the dissociation equilibrium constant for O2 binding (Ko2) for Y each hemoglobin and to show the difference in the extent of allo- stery or cooperativity of subunit interaction in each type of hemo- globin. 0.4 You need draw only the central, linear portion of the Hill plot. 0.2 F State what is the likely magnitude of the Hill constant (nH) for HbA from your reading and state what is the likely range of the magni- tude of the Hill coefficient for Hb Great Lakes. 0 10 20 30 40 50 60 pO2 (torr)1.12 At elevated altitudes, the body adapts to the reduced barometric pressure to extract sufficient oxy- gen to permit normal metabolic functions and do work. For example, at an altitude of 3,650 m (close to 12,000 feet above sea level) the barometric pressure drops to 485 mmHg. For an oxygen pressure drop in the lungs of 30 mmHg, determine the oxygen uptake rate for a respiration rate of 20 breaths per minute. Estimate the oxygen saturation in venous blood if the hematocrit rises to 0.60 and the partial pressure of oxygen blood is at a partial pressure equal to 98% of the alveolar level.
- Carbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!On the right the Hill plot com- (b) pares the O2 binding properties of Hb Ya- kima with those of HbA in 0.1 M NaCl buff- Hb-Yakima ered to pH 7 with 0.01 M bis-Tris. Focus first on the line for "stripped Hb". This is the term for hemoglobin isolated from erythro- cytes with removal of all organic phosphate molecules that might bind to the protein in RBCS. You can see that 2,3-bisphospho- glycerate (BPG; labeled DPG according to old terminology) does not alter the O2 bind- ing affinity of Hb Yakima in contrast to HbA (although it was shown that BPG did bind to the deoxyHb Yakima molecule). Also, Hb Yakima is associated with markedly decreased allostery in the absence and presence of BPG, in comparison to HbA. IHP = inositol hexaphosphate, an artificial allosteric modifying ligand that binds more tightly than BPG. stripped Hb Hb-A •DPG +DPG n= 1.0 n = 2.3 n=2,5 +THP +IHP 0.5 0.5 1 5 10 50 po, ( mm Hg ) %3D On the right is a diagram copied from the lecture handout "Hemoglobin and Allo-…ΔG°′ for the isomerization reaction glucose-1-phosphate (G1P) ⇌ glucose-6-phosphate (G6P) is −7.1 kJ · mol−1. Calculate the equilibrium ratio of [G1P] to [G6P] at 25°C.
- The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.PTP1B Substrate kcat Km kcat/Km UM 10-7 x (s-1 M) DADEPYLIPQQG DADAPYLIPQQG DAAEPYLIPQQG AAAAPYLIPQQG 44.6 + 1.8 39.8 + 0.32 3.9 + 0.9 13.7 + 0.46 1.1 + 0.25 0.29 + 0.01 35.3 + 0.22 6.6 ± 0.22 0.53 + 0.02 34.7 + 0.25 52.7 ± 0.7 0.066 + 0.001 (d) (. ) The units for kcat/KM in the above are given according to standard scientific notation. On this basis what is the value of this kinetic parameter for the DADEPYLIPQQG substrate?Acid phosphatases are an important group of enzymes that can be detected in human bloodserum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyzebiological phosphate esters as follows:R-O-P-O3-2 + H2O -----> R-OH + HO-P-O3-2Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver,and prostrate gland. The enzyme from the prostrate gland is clinically important because anincreased activity in the blood is frequently an indication of cancer of the prostrate gland.Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acidphosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostrate gland in humanblood serum?
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