Complete cDNA sequence for rabbit muscle glycogen phosphorylase
نویسندگان
چکیده
منابع مشابه
Complete amino acid sequence of rabbit muscle glycogen phosphorylase.
The sequence of the 841 amino acid residues in each subunit (molecular weight 97,412) of rabbit muscle glycogen phosphorylase b (1,4-alpha-D-glucan:orthophosphate alpha-glucosyltransferase; EC 2.4.1.1) has been determined. The general strategy was based on limited proteolysis of native phosphorylase b by subtilisin BPN', yielding two large segments (light and heavy) which were fragmented by cle...
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 کاملRabbit skeletal muscle phosphorylase kinase. Comparison of glycogen synthase and phosphorylase as substrates.
The Ca”-stimulated phosphorylation of rabbit muscle glycogen synthase (EC 2.4.1.11) catalyzed by phosphorylase kinase (EC 2.7.1.38) was characterized and compared with the reaction involving phosphorylase (EC 2.4.1.1). By comparing reaction rates at equal concentrations (on a mass basis), the activity ratio of phosphorylase/synthase varied from 30 (0.05 mg/ml) to approximately 8 (1 mg/ml). A ba...
متن کاملRabbit Skeletal Muscle Glycogen
Glycogen in its particulate beta-form is localized in the sarcoplasm close to the sarcoplasmic reticulum. Some particles are in close contact with the membranes, on the outer side of the vesicles. The mild technique of differential precipitation-centrifugation has been adapted to the preparation of glycogen from adult skeletal muscle. A preliminary low-speed centrifugation which eliminates the ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1986
ISSN: 0014-5793
DOI: 10.1016/0014-5793(86)80829-8