Phosphorylase kinase conformers. Detection by proteases.
نویسندگان
چکیده
منابع مشابه
Liver Phosphorylase Kinase
a deficiency of liver phosphorylase kinase, causing a lack of active glycogen phosphorylase, although total phosphorylase is normal. The intravenous injection of glucagon caused a rapid activation of cyclic AMP-dependent protein kinase in the liver, but no increase in either phosphorylase kinase or phosphorylase a activity. Although total glycogen synthase activity in the livers of affected rat...
متن کاملLiver Glycogen Phosphorylase Kinase
Liver glycogen phosphorylase kinase was assayed by measuring the radioactivity of [y-32P]ATP incorporated into rabbit skeletal muscle phosphorylase b. Using this assay two forms of phosphorylase kinase, Kinase I and Kinase II, were pirified about 70and 130-fold, respectively, from rabbit liver cytosol by DEAE-Sephadex A50 column chromatography, ammonium sulfate fractionation, gel filtration on ...
متن کاملCardiac Phosphorylase Kinase
We have documented previously that although the phosphorylation of the p subunit of cardiac phosphorylase kinase plays a major role in activation of the enzyme, enzyme activity is also modulated by either CAMP-dependent or CAMP-independent phosphorylation of the a’ subunit (Sul, H. S., Cooper R. H., Whitehouse s., and Walsh D. A. (1982) J. Biol. Chem. 257, 3484-3490). This paper reports that de...
متن کاملMycoplasma pneumoniae HPr kinase/phosphorylase.
HPr kinase/phosphorylase (HPrK/P) is the key regulator of carbon metabolism in many Gram-positive bacteria. It phosphorylates/dephosphorylates the HPr protein of the bacterial phosphotransferase system on a regulatory serine residue in response to the nutrient status of the cell. In Mycoplasma pneumoniae, HPrK/P is one of the very few regulatory proteins encoded in the genome. The regulation of...
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)...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)61352-3