Calcium‐calmodulin‐dependent activation of porcine liver phosphorylase kinase

FEBS Letters

Mizuta, K.¹  Hashimoto, E.¹  Tsutou, A.¹  Yamamura, H.¹  Nakamura, S.¹  Negami, A.¹  Nakaza, T.¹ 

[1] Department of Biochemistry, Fukui Medical School, Matsuoka, Fukui 910-11, Japan

关键词: Phosphorylase kinase;    Calcium;    Calmodulin;    Porcine liver;    Epinephrine;    Glycogen metabolism;    EGTA;    ethylene glycol bis-(β-aminoethyl ether)-N;    N;    N';    N'-tetraacetic acid;    PMSF;    phenylmethylsulfonyl fluoride;   

DOI  :  10.1016/0014-5793(83)80414-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Porcine liver phosphorylase kinase was activated about 1.5-fold by calmodulin in a calcium-dependent manner. Half-maximal stimulation was observed at about 80 nM calmodulin and the activation was almost pH-independent. The specific binding of procine liver phosphorylase kinase to calmodulin—Sepharose affinity column exhibited an absolute dependence upon the presence of calcium. The physiological role of the calmodulin-dependent activation for liver phosphorylase kinase is discussed.

【 授权许可】

Unknown