A novel glycogen synthase phosphatase from canine heart

Two molecular forms (M r=49,300 and 26,000) of a divalent cation-dependent (Mg 2+=Mn 2+>Co 2+) protein phosphatase, which represent the major glycogen synthase phosphatase activity in canine heart extracts, have been partially purified and characterized. Although a general protein phosphatase of...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 87; no. 4; pp. 1226 - 1234
Main Authors Feigenbaum Binstock, Judith, Li, Heng-Chun
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 27.04.1979
Subjects
Animals
Dogs
Glycogen-Synthase-D Phosphatase - isolation & purification
Glycogen-Synthase-D Phosphatase - metabolism
Kinetics
Magnesium - pharmacology
Molecular Weight
Myocardium - enzymology
Phosphoprotein Phosphatases - metabolism
Rabbits
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Summary:Two molecular forms (M r=49,300 and 26,000) of a divalent cation-dependent (Mg 2+=Mn 2+>Co 2+) protein phosphatase, which represent the major glycogen synthase phosphatase activity in canine heart extracts, have been partially purified and characterized. Although a general protein phosphatase of M r=35,000 is also active toward synthase D, it represents the major phosphorylase phosphatase activity in heart muscle. The present findings indicate that the dephosphorylation of synthase D and phosphorylase a may be regulated by two distinct phosphatases rather than by a single nonspecific enzyme.
Bibliography:L
L50
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SourceType-Scholarly Journals-1
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ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(79)80038-8