منابع مشابه
Rabbit 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 ...
متن کاملHormonal regulation of glycogen synthase phosphorylation in rabbit skeletal muscle.
Phosphorylation of rabbit skeletal muscle glycogen synthase in vivo in response to hormones was investigated. Methods were developed to purify the synthase without altering its kinetic parameters, thereby indicating constancy of the synthase phosphorylation state. The enzyme from control rabbits had an activity ratio (-glucose-6-P/+glucose-6-P) of 0.24, K, for glucose-6P of 0.17 m ~ , and K , f...
متن کاملStructural Studies on Rabbit Muscle Glycogen Synthase
Limited tryptic digestion of either synthase I or D forms resulted in the appearance of a new glucose 6-phosphate-dependent form which was composed of 75,000 molecular weight subunits. Early in tryptic digestion, an intermediate 78,000 subunit was also observed with both forms of the enzyme. The NH,terminal dipeptide sequence of the 75,000 subunit of both forms was the same as that of the origi...
متن کاملGlycogen as a fuel for skeletal muscle.
The utilization of glycogen by skeletal muscle was, at one time, one of the central problems of biochemistry. Attention focused on the most dramatic property of the system: the very rapid glycogenolysis that occurs synchronously with muscle contraction. This phenomenon now has a generally accepted explanation : the increase in Ca2+ that induces muscle contraction also activates phosphorylase ki...
متن کاملPhosphorylation of glycogen synthase by cyclic AMP-independent casein kinase-2 from rabbit skeletal muscle.
Cyclic AMP-independent casein kinase-2 from rabbit skeletal muscle has been extensively purified by procedures including phosphocellulose, Bio-Gel A-1.5m, casein-Sepharose, and DEAE-cellulose column chromatographies. The casein kinase and glycogen synthase kinase activities are co-purified throughout the purification. The casein kinase-2 has Mr approximately equal to 135,000 as determined by gl...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 1968
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.38.1.130