An Adenosine 3′,5′-Monophosphate-dependant Protein Kinase from Rabbit Skeletal Muscle
نویسندگان
چکیده
منابع مشابه
Studies on the adenosine 3',5'-monophosphate-dependent protein kinases of rabbit skeletal muscle.
The adenosine 3’,5’-monophosphate-dependent (CAMPdependent) protein kinases of rabbit skeletal muscle have been partially characterized in terms of molecular size and subunit composition. Three and possibly four species of protein kinase have been detected. The largest form of the enzyme was estimated by gel filtration and sedimentation to have a molecular weight of 123,000 and to be made up of...
متن کاملPurification and properties of rabbit skeletal muscle adenosine 3',5'-monophosphate-dependent protein kinases.
A modified procedure for purification of the adenosine 3’,5’-monophosphate-dependent (cyclic AMP-dependent) protein kinase from rabbit skeletal muscle is described. This procedure results in the separation of the enzyme into two peaks of activity on diethylaminoethylcellulose. No interconversion of these two peaks was observed. Both peaks exhibit dependence on cyclic AMP, but under certain cond...
متن کاملPurification and characterization of catalytic subunit of skeletal muscle adenosine 3':5'-monophosphate-dependent protein kinase.
The catalytic subunit of rabbit skeletal muscle cyclic adenosine 3':5'-monophosphate-dependent protein kinase has been isolated in pure form. It has a molecular weight of 41,300, as determined by sedimentation equilibrium, which is in good agreement with the value of 41,000 determined by electrophoresis in the presence of sodium dodecyl sulfate. Sedimentation velocity determinations indicate th...
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suggesting the rapid formation of one or more complexes (C) between the two proteins within which electron transfer takes place. Attempts to detect directly the presence of a thermodynamically stable complex between the various forms of the two proteins are presently being carried out. An explanation of the mechanism of electron transfer between azurin and cytochrome 551, in analogy with lines ...
متن کاملActivation of skeletal muscle phosphorylase kinase by adenosine triphosphate and adenosine 3',5'-monophosphate.
Rabbit skeletal muscle phosphorylase kinase has been obtained as a nearly homogeneous protein showing a single peak on electrophoresis and in the ultracentrifuge. Incubation of the purified kinase with T~~P-ATP in the presence of Mg++ ions activates the enzyme; this process is accompanied by phosphorylation of the protein. Activation and phosphorylation of phosphorylase kinase occur more rapidl...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)34204-8