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Resolution of Ca2+—calmodulin‐activated protein kinase from wheat germ
[摘要]

A soluble Ca2+- and Ca2+—calmodulin-activated protein kinase was partially purified from wheat germ. The phosphorylation of histones and casein catalyzed by this enzyme is largely Ca2+-dependent. After repeated gel filtration of the protein kinase in the presence of 1 mM EGTA, the phosphorylation of casein and histones by the enzyme is activated 3-fold and up to 16-fold, respectively, by added calmodulin (12.5 μM). Such activation of the protein kinase by calmodulin is Ca2+-dependent. The protein kinase binds to calmodulin—Sepharose 4B in a Ca2+-dependent fashion. This type of Ca2+-activated protein kinase may be involved in stimulus—response coupling in plants.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[关键词] Calmodulin;Protein kinase;Wheat germ;Histone;Calcium;Phenothiazine;cyclic AMP;adenosine 3′;5′-monophosphate;CAPP;2-chloro-10-(3-aminopropyl) phenothiazine [时效性] 
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