Table 2.18 Dissociation Constants of Some Bioaffinity Interactions Ligand-Receptor Pair Kp (M) Enzyme-substrate Lectin-monosaccharide 10-5 10-3. 10 Lectin-oligosaccharide Antibody-antigen DNA-protein Cell receptor-ligand Avidin/Streptavidin-biotin 10-5 10-5 - 10-7 10-7 - 10-11 10-8 - 10-9 10-9 - 10-12 ~10-15

Table 2.18 Dissociation Constants of Some Bioaffinity Interactions Ligand-Receptor Pair Kp (M) Enzyme-substrate Lectin-monosaccharide 10-5 10-3. 10 Lectin-oligosaccharide Antibody-antigen DNA-protein Cell receptor-ligand Avidin/Streptavidin-biotin 10-5 10-5 - 10-7 10-7 - 10-11 10-8 - 10-9 10-9 - 10-12 ~10-15

Chemistry for Today: General, Organic, and Biochemistry

9th Edition

ISBN:9781305960060

Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Chapter20: Enzymes

Section: Chapter Questions

Problem 20.26E

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Similar questions

The human body has an average pH of about 7 and a temperature of about 37C. Use graphs to illustrate enzyme activity in the human body as a function of the following: a. Substrate concentration b. Enzyme concentration c. pH include pH optimum value d. Temperature include temperature optimum value
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Does Km value change with an increase of enzyme concentration? Explain
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From the given activity, 1.) What is the effect of temperature to the enzyme? 2.) What are some generalizations and conclusions in this activity?
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I don’t understand how to do part b of question 5. The other picture is my work of part a. How would changing the enzyme concentration affect Km and Vmax. The answer given to us is Vo= 0.796mM/s. I just don’t understand how to get to that answer.
An antibody X binds to an antigen Y. When the antigen concentration is 8.0× 10–8 M, θ is 0.90. What is the dissociation constant, Kd, of the antibody for the antigen?
4. The amino acid Asp189 lies at the base of the substrate specificity pocket in the enzyme trypsin. a. How is this related to typsin’s substrate specificity? Briefly describe the interactions between the substrate and the Asp 189. b. If the Asp189 was replaced with a lysine residue, how would this affect substrate specificity? c. The scientists that actually mutated the Asp189 to a lysine analyzed the three-dimensional structure of the enzyme and found that the lysine is actually not located in the specificity pocket. Instead, the Lys side chain reaches out of the base of the pocket, rendering the pocket nonpolar. With this additional information, determine how the substrate specificity would differ in the lysine-mutated enzyme.
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