منابع مشابه
Kinetic mechanism of potato phosphorylase.
Polysaccharide phosphorylase isolated from Idaho potatoes was the subject of a steady state kinetic study. The initial velocity of the reaction between a-D-glucopyranose l-phosphate (glucose-l-P) and amylopectin, in the absence of orthophosphate, was determined as a function of substrate concentration. A similar study was carried out for the reverse reaction. The result is characteristic of a s...
متن کاملOn the mechanism of action of muscle and potato phosphorylase.
It has recently been reported by Doudoroff, Barker, and Hassid (1) t’hat an exchange occurs between the phosphate group of glucose-l-phosphate and inorganic phosphate in the presence of sucrose phosphorylase and in the absence of acceptor. On the basis of this exchange, they postulate a mechanism involving the formation of an enzyme-glucose complex, thus endowing the enzyme wit,h the ability to...
متن کاملStarch Phosphorylase of Potato
Cori and his colleagues (l-6) discovered and elucidated the series of reversible chemical reactions by which glucose is transformed into glycogen in animal tissues. These reactions are catalyzed by a group of enzymes, the most fundamental of which is phosphorylase, the enzyme which catalyzes the condensation of glucose-l-phosphate (Cori ester) to starch or glycogen. The properties of phosphoryl...
متن کاملKinetic mechanism of rabbit muscle glycogen phosphorylase a.
Isotope-exchange rates at chemical equilibrium were determined for the glycogen-a-D-glucopyranose l-phosphatePi system in the presence of phosphorylase a. Exchange of 32P from a-n-glucopyranose l-phosphate (glucose-l-P) into Pi and exchange of 14C from glucose-l-P into glycogen were followed simultaneously by the use of glucose-l-P containing both isotopes. Concentrations of glucose-l-P and Pi ...
متن کاملStarch phosphorylase inhibitor from sweet potato.
A protein, starch phosphorylase inhibitor, was purified from the root of sweet potato (Ipomoea batatas [L.] Lam. cv Tainon 65). It had a molecular weight of 250,000 and could be composed of five identical subunits. The isoelectric point of the inhibitor was 4.63. It was a noncompetitive inhibitor toward the sweet potato enzyme with a K(i) value of 1.3 x 10(-6) molar when glucose-1-P was the var...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62150-7