Post-translational phosphorylation of proteodermatan sulfate.
نویسندگان
چکیده
منابع مشابه
Proteodermatan sulfate isolated from pig skin.
The major proteoglycan of pig skin, a proteodermatan sulfate, has been isolated under mild conditions in the presence of protease inhibitors. After purification by ion exchange and gel chromatography, it has a Mr of 70 x 10(3) and it does not form aggregates with hyaluronic acid. It contains about 60% protein, one chain of dermatan sulfate, and several oligosaccharide chains. The dermatan sulfa...
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Proteodermatan sulfate was extracted from four areas of the bovine gastrointestinal tract (esophagus, stomach, small intestine and colon) with 4 M guanidine-HCl and then purified by ion-exchange and gel filtration chromatography. Dermatan sulfate chains which made up proteodermatan sulfate from each area were separately prepared by Pronase P and endo-beta-xylosidase digestion. The properties of...
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Secondary shifts develop in post-translational phosphorylation of sarcomeric proteins in multiple animal models of inherited cardiomyopathy. These signaling alterations together with the primary mutation are predicted to contribute to the overall cardiac phenotype. As a result, identification and integration of post-translational myofilament signaling responses are identified as priorities for ...
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In vitro phosphorylation of purified human plasma apolipoprotein A-I (apoA-I) by a recently characterized Ca2+/calmodulin-dependent kinase (Beg, Z. H., Stonik, J. A., and Brewer, H. B., Jr. (1987) J. Biol. Chem. 262, 13228-13240) was time-, Ca2+-, and calmodulin-dependent. Maximal phosphorylation of human apoA-I revealed a stoichiometry of approximately 1 mol of PO4/mol of apoA-I. Phosphorylati...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1986
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)36030-1