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

FEBS Letters

Davies, Jeffrey R.¹  Polya, Gideon M.¹ 

[1] Department of Biochemistry, La Trobe University, Bundoora, VIC 3083,Australia

关键词: Calmodulin;    Protein kinase;    Wheat germ;    Histone;    Calcium;    Phenothiazine;    cyclic AMP;    adenosine 3′;    5′-monophosphate;    CAPP;    2-chloro-10-(3-aminopropyl) phenothiazine;   

DOI  :  10.1016/0014-5793(82)81327-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown