Phosphorylation of caldesmon by p34cdc2 kinase. Identification of phosphorylation sites.
نویسندگان
چکیده
منابع مشابه
Phosphorylation of smooth muscle caldesmon by calmodulin-dependent protein kinase II. Identification of the phosphorylation sites.
Smooth muscle caldesmon was phosphorylated by smooth muscle calmodulin-dependent protein kinase II. The extent of phosphorylation obtained was 5.65 mol of phosphate/mol of caldesmon. Phosphorylated protein was subjected to the complete trypsin proteolysis and the produced phosphopeptides were purified by C-8 reverse phase chromatography. Nine phosphopeptides were isolated and by amino acid sequ...
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Phosphorylation of human CTP synthetase 1 by mammalian protein kinase C was examined. Using purified Escherichia coliexpressed CTP synthetase 1 as a substrate, protein kinase C activity was timeand dose-dependent and dependent on the concentrations of ATP and CTP synthetase 1. The protein kinase C phosphorylation of the recombinant enzyme was accompanied by a 95-fold increase in CTP synthetase ...
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The CHO1-encoded phosphatidylserine synthase from Saccharomyces cerevisiae is phosphorylated and inhibited by protein kinase A in vitro. CHO1 alleles bearing Ser(46) --> Ala and/or Ser(47) --> Ala mutations were constructed and expressed in a cho1Delta mutant lacking phosphatidylserine synthase. In vitro, the S46A/S47A mutation reduced the total amount of phosphorylation by 90% and abolished th...
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Polarity along the anteroposterior axis of the Drosophila embryo is established by the activity of maternal gene products deposited into the egg during oogenesis. These activities direct specialised domains of zygotic gene expression required for the determination of cell fate (St. Johnston and Nüsslein-Volhard, 1992). The anterior system, which is required for the formation of the head and the...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)54878-x