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Limited proteolysis of 3‐phosphoglycerate kinase without loss of enzymic activity
Author(s) -
Jiang Shu-Xian,
Vas Mária
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80721-x
Subject(s) - proteolysis , phosphoglycerate kinase , chemistry , biochemistry , enzyme , trichloroacetic acid , kinetics , covalent bond , digestion (alchemy) , phosphoglycerate mutase , chromatography , glycolysis , physics , organic chemistry , quantum mechanics
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.