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

Shu Xian Jiang, M. Vas

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)151-154
Number of pages4
JournalFEBS Letters
Volume231
Issue number1
DOIs
Publication statusPublished - Apr 11 1988

Fingerprint

Proteolysis
Phosphoglycerate Kinase
Molecular mass
Digestion
Trichloroacetic Acid
Peptides
Molecules
Enzymes
Muscle
Polyacrylamide Gel Electrophoresis
Swine
Adenosine Triphosphate
Muscles
Kinetics
Substrates
3-phosphoglycerate

Keywords

  • (Pig muscle)
  • 3-Phosphoglycerate effect
  • 3-Phosphoglycerate kinase
  • Tryptic digestion

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Limited proteolysis of 3-phosphoglycerate kinase without loss of enzymic activity. / Jiang, Shu Xian; Vas, M.

In: FEBS Letters, Vol. 231, No. 1, 11.04.1988, p. 151-154.

Research output: Contribution to journalArticle

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