PHOSPHORYLASE ACTIVITY OF SKELETAL MUSCLE EXTRACTS
نویسندگان
چکیده
منابع مشابه
Phosphorylase Activity in Rat Liver and Skeletal Muscle after Catecholamines.
The tune course of liver phosphorylase activation after catecholamine administration and the relative abilities of several adrenergic blocking agents to block catecholamine-induced phosphorylase activation in liver and skeletal muscle was studied in intact anesthetized rats. Subcutaneously injected epinephrine and norepinephrine increased the liver phosphorylase activity, the peak effect occurr...
متن کاملPhosphofructokinase activity in skeletal muscle extracts following administration of epinephrine.
Phosphofructokinase in rabbit skeletal muscle was assayed before and after intravenous epinephrine administration. Assays at optimal pH (8.2) and in the presence of optimal substrate concentrations showed no significant difference in enzyme activity. Muscle extracts prepared in the presence of caffeine were assayed under conditions optimal for allosteric kinetics (pH 6.9 and low substrate conce...
متن کاملPhosphofructokinase Activity in Skeletal Muscle Extracts following Administration of Epinephrine*
Phosphofructokinase in rabbit skeletal muscle was assayed before and after intravenous epinephrine administration. Assays at optimal pH (8.2) and in the presence of optimal substrate concentrations showed no significant difference in enzyme activity. Muscle extracts prepared in the presence of caffeine were assayed under conditions optimal for allosteric kinetics (pH 6.9 and low substrate conce...
متن کاملThe regulation of skeletal muscle phosphorylase kinase by Ca2+.
The interaction between highly purified rabbit muscle phosphorylase kinase and CaZf has been investigated and this metal has been shown to be necessary for enzyme activity. Utilizing caldum-free reagents, apparent Km values for Ca2f were determined for the activated kinase (2 x 10’ M at pH 8.2, 5 x 10e7 M at pH 6.8) and for the nonactivated kinase (3 X lob6 M at pH 8.2, indeterminate at pH 6.8)...
متن کاملPhosphorylase kinase phosphorylation of skeletal-muscle troponin T.
Rabbit skeletal-muscle troponin T was phosphorylated by a standard preparation of phosphorylase kinase [Cohen (1973) Eur. J. Biochem. 34, 1--14] and by fractions obtained after chromatography of phosphorylase kinase on phosphocellulose. The original preparation of phosphorylase kinase phosphorylated at least two sites, one of which was serine-1. The second and probably the third sites were pres...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1955
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)52288-8