Two diverse effects of poly(L‐lysine) on rabbit skeletal muscle phosphorylase kinase: stimulation of autophosphorylation and inhibition of its activity

FEBS Letters

Kobayashi, Tomoko¹  Nakamura, Shun-ichi¹  Negami, Akira¹  Yamamura, Hirohei¹  Sakai, Kuniyasu¹  Tabuchi, Hikaru¹ 

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

关键词: Glycogen phosphorylase kinase;    Autophosphorylation;    Polylysine;    Rabbit skeletal muscle;    protein kinase A;    cAMP-dependent protein kinase;    SDS;    sodium dodecyl sulfate;    buffer A;    50 mM α-glycerophosphate (pH 6.8);    2 mM EDTA and 10 mM 2-mercaptoethanol;    Hepes;    N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid;   

DOI  :  10.1016/0014-5793(84)80107-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Polylysine greatly stimulated the autophosphorylation of phosphorylase kinase from rabbit skeletal muscle. When fully autophosphorylated, about 14 mol of phosphate per tetramer (αβγδ) were incorporated in the presence of polylysine, which was twice as much as those observed without polylysine. In contrast to this stimulatory effect of polylysine on the autophosphorylation, polylysine strongly inhibited the conversion reaction of phosphorylase b to a. The inhibition is competitive with a K _i of 2.3 μg/ml. No effects of polylysine were observed on the activities of phosphorylase and cAMP-dependent protein kinase.

【 授权许可】

Unknown