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Subcellular localization of LH-dependent phosphoproteins and their possible role in regulation of steroidogenesis in rat tumour Leydig cells |
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| Authors: | G H Bakker J W Hoogerbrugge F F Rommerts H J van der Molen |
| Institution: | 1. Department of Chemistry, Faculty of Science, Nara Women''s University, Nara 630 Japan;2. Department of Chemistry, Kyoto University of Education, Kyoto 612, Japan;3. Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611, Japan |
| Abstract: | Yeast phosphorylase is phosphorylated and activated by a cyclic AMP-independent protein kinase (called phosphorylase kinase) and a cyclic AMP-dependent protein kinase. Only in the presence of both kinases is phosphorylase fully activated and phosphorylated. No evidence was found for the presence of two phosphorylation sites as an identical phosphopeptide pattern of phosphorylase is obtained after phosphorylation by either one or both kinases. The kinases probably phosphorylate identical sites but recognize different subunits of phosphorylase. Phosphorylase kinase phosphorylates the high-Mr subunit while cAMP-dependent protein kinase phosphorylates the low-Mr subunit. |
| Keywords: | D-Glucosaminate dehydratase α β-Elimination reaction Pyridoxal 5'-phosphate Proton NMR analysis Stereochemistry |
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