The isoelectric point, pI, of the protein hexokinase P-I is 5.25, while that of alkaline phosphatase is 4.5 What is the net charge of hexokinase P-I at pH 5.1 ?| What is the net charge of alkaline phosphatase at pH 2.1 ?[ The isoelectric point of glycine is 5.97; threonine, 5.6. During paper electrophoresis at pH 7.1, toward which electrode does glycine migrate? During paper electrophoresis at pH 4.5, toward which electrode does threonine migrate?

The isoelectric point, pI, of the protein hexokinase P-I is 5.25, while that of alkaline phosphatase is 4.5 What is the net charge of hexokinase P-I at pH 5.1 ?| What is the net charge of alkaline phosphatase at pH 2.1 ?[ The isoelectric point of glycine is 5.97; threonine, 5.6. During paper electrophoresis at pH 7.1, toward which electrode does glycine migrate? During paper electrophoresis at pH 4.5, toward which electrode does threonine migrate?

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter23: Enzymes

Section: Chapter Questions

Problem 23.35P

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An enzymatic assay was performed using the enzyme phophofructokinase-1, which catalyses the committed step of the glycolysis pathway. What is the final concentration of the fructose 6-phosphate substrate in a test tube containing the following: 250 µL of 150pM fructose 6-phophate, 100 µL 20 mg.ml-1 phosphofructoskinase-1 and 150 µL 100mM buffer pH 7.5
At a steady state in the living cell, (ATP) = 10-3M and (ADP) = 10-4 M. The maximum(equilibrium) value of the ratio (glycerol-1-P)/(glycerol) is observed to be 770 at 25 Cand pH=7.a. Calculate K and rG for the reaction.b. Using the value of rG for the reaction ADP + Pi →ATP + H2O, together with the answer topart (a), calculate rG and K for the reaction: glycerol + phosphate→ glycerol-1-phosphate+ H2O
In one of the steps in this pathway fructose 1,6-biphosphate (F1,6BP) is converted to gylceraldehyde-3-phosphate (G-3-p) and dihydroxyacetone phosphate (DHAP). This reaction is catalyzed by the enzyme aldolase. For this reaction at 25 celcuius and Ph7 we have: Keq= 10-4M and Delta G = +5456 cal/mol Calculate the following: The concentration of F1, 6BP, DHAP and G-3-P at equilibrium when the initial F1,6BP is (A) 1M, (b) 10-2 M, (c) 2 X 10*4 M and (d) 10-5 M. I been trying to solve this problem but I dont even know where to begin with. Atleast help me with problem A, I would be able to guide myself through.
3) The enzyme aldolase catalyzes the conversion of fructose-1,6-diphosphate (FDP)to dihydroxyacetone phosphate (DHAP) and glyceraldehide-3-phosphate (G3P). Thereaction isFDP ⇄ DHAP + G3P , ∆rG0(298.15 K) = 23.8 kJ mol−1In red blood cells the concentration of these species are [FDP] = 35 µM, [DHAP] =130 µM, and [G3P] = 15 µM. (Remember that 1.0 µM = 1.0 × 10−6 mol L−1. Thestandard state for reactions in solution can be taken as c0 = 1.0 mol L−1).Calculate ∆rG in a red blood cell at 25 0C. Will the reaction occur spontaneouslyin the cell at this temperature?
Assume that in a certain cell, the ratio of products/reactants or Keq = 614.9 (Keq is dimensionless) for the reaction Glucose + ATP <> Glucose-6-P + ADP, at a particular instant, the concentrations of each compound were Glucose =4.3M, ATP =10.5M, ADP =17.3M and G-6-P =23.5M. Calculate the difference (dimensionless) between Keq and the ratio of products/ractants at this instance, in this cell, to five significant figures.
Help with the following question Ksp for AgCO3 is 8.46x10^-12
The Ksp for AG2SO4 is 1.2x10^-5 and the Ksp for CaSO4 is 4.93x10^-5. How do I find the Ca concentration?
If, in addition to the constraints on glucose concentration listed previously, we have in the liver cell ATP concentration = 1 mM and ADP concentration == 3 mM, what is the theoretical concentration of glucose-6-phosphate at equilibrium at pH=7.4 and 37 ∘C?
The equilibrium constant, Keq, for the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP) is 0.0475 under standard conditions (298 K, 1 atm, pH 7). Calculate ∆G ̊’ for the reaction. What is ∆G’ for the isomerization reaction when the initial concentrations of DHAP and GAP are 2.2 ́ 10-4 M and 2.9 ́ 10-6 M, respectively? Assume a temperature of 298 K. The same enzyme catalyzes the reverse reaction, the isomerization of GAP to form DHAP. Assume the concentration of GAP remains constant at 2.9 ́ 10-6 M. What is the maximum concentration of DHAP that allows the reaction to proceed spontaneously in this direction?
Based on the graphical information in Problem 21-41 about enzymes A and B a. What is the optimum pH for enzyme B? b. What is the optimum temperature for enzyme A? c. Which enzyme has the greater activity at a pH of 7.2? d. Which enzyme has the greater activity at a temperature of 37.2C?
(a) Describe in detail how you will determine the primary structure of protein. (b)You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows:Histidine 7.64Lysine 9.74Cystenie 5.02Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.