Limited proteolysis of 3‐phosphoglycerate kinase without loss of enzymic activity

FEBS Letters

Vas, Mária¹  Jiang, Shu-Xian¹ 

[1] Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest H-1502, PO Box 7, Hungary

关键词: Tryptic digestion;    3-Phosphoglycerate effect;    3-Phosphoglycerate kinase;    (Pig muscle);    PGK;    3-phosphoglycerate kinase (EC 2.7.2.3);    3-PG;    3-phosphoglycerate;    BAEE;    benzoyl-L-arginine ethyl ester;    PMSF;    phenylmethylsulfonyl fluoride;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(88)80721-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

During tryptic digestion of pig muscle 3-phosphoglycerate kinase in the presence of 3-phosphoglycerate both the decrease of enzymic activity and the release of trichloroacetic acid-soluble peptides occur after a pronounced lag period. During this lag phase the native enzyme molecule is split into two fragments with molecular masses of about 30 and 18 kDa, as detected by SDS-PAGE. Under non-denaturing conditions, however, these fragments are held together by non-cova-lent forces and constitute an active, nicked enzyme molecule. In the absence of substrates or in the presence of MgATP the kinetics of tryptic digestion is apparently a single first order reaction leading to the formation of peptides with molecular masses of less than 10 kDa.

【 授权许可】

Unknown