The CAMP formed by adenyl cyclase does not persist because 5- Phosphodiesterase activity prevalent in cells hydrolyzes CAMP to give 5'-AMP. Caffeine inhibits 5'-Phosphodiesterase activity which promotes the presence of the more active 'a' form of Glycogen Phosphorylase. a If no precautions are taken blood that has been stored for some time becomes depleted in 2-3 BPG which will result in increased binding of 02 to Hemoglobin with decreased release of 0, to tissues. Sickle-cell anemia is the consequence of HbS polymerization through hydrophobic contacts between the side chain Vala6 and a pocket in the EF corner of a-subunits. d. Decreasing the free energy of activation increase the reaction rate. The catalytic efficiency of an enzyme cannot exceed the diffusion rate e of encounters between E and S. f When [S] = Km the velocity = Vmax/2. Lineweaver-Burk double reciprocal (1/V vs. 1/S) plots convert the g hyperbolic Michaelis-Menten V vs. S plot into a straight line. According to the Michaelis-Menten equation the v/Vmax ratio = 0.4 when [S] = 4 Km: If Vmax = 100 umol/mL/sec and Km = 2 mM the velocity of the reaction i when [S] = 20 mM is 10 umol/mL/sec.
The CAMP formed by adenyl cyclase does not persist because 5- Phosphodiesterase activity prevalent in cells hydrolyzes CAMP to give 5'-AMP. Caffeine inhibits 5'-Phosphodiesterase activity which promotes the presence of the more active 'a' form of Glycogen Phosphorylase. a If no precautions are taken blood that has been stored for some time becomes depleted in 2-3 BPG which will result in increased binding of 02 to Hemoglobin with decreased release of 0, to tissues. Sickle-cell anemia is the consequence of HbS polymerization through hydrophobic contacts between the side chain Vala6 and a pocket in the EF corner of a-subunits. d. Decreasing the free energy of activation increase the reaction rate. The catalytic efficiency of an enzyme cannot exceed the diffusion rate e of encounters between E and S. f When [S] = Km the velocity = Vmax/2. Lineweaver-Burk double reciprocal (1/V vs. 1/S) plots convert the g hyperbolic Michaelis-Menten V vs. S plot into a straight line. According to the Michaelis-Menten equation the v/Vmax ratio = 0.4 when [S] = 4 Km: If Vmax = 100 umol/mL/sec and Km = 2 mM the velocity of the reaction i when [S] = 20 mM is 10 umol/mL/sec.
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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