Phosphorylation of mylein basic protein by glycogen phosphorylase kinase

FEBS Letters

Kobayashi, Tomoko¹  Nakamura, Shun-ichi¹  Negami, Akira¹  Nakaza, Toshiko¹  Yamamura, Hirohei¹ 

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

关键词: Glycogen phosphorylase kinase;    Mylein basic protein;    Rabbit skeletal muscle;    cAMP-dependent protein kinase;    Phk;    glycogen phosphorylase kinase;    MBP;    myelin basic protein;    protein kinase A;    cAMP-dependent protein kinase;    HPLC;    high-performance liquid chromatography;   

DOI  :  10.1016/0014-5793(84)80323-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ability of homogeneous glycogen phorphorylase kinase (Phk) from rabbit skeletal muscle to phosphorylate bovine brain myelin basic protein (MBP) was investigated. Phk could incorporate a maximum of 1.9 mol phosphate/mol MBP. The apparent K _m and V _max for Phk phosphorylation of MBP were 27 μM and 90 nmol/min per mg enzyme, respectively. Properties of MBP phosphorylation by Phk are similar to those of phosphorylase as a substrate. Only serine residues of MBP are phosphorylated by Phk. Phosphorylation sites of MBP by Phk are not identical to those by cAMP-dependent protein kinases.

【 授权许可】

Unknown