Kinetic behaviour and oligomeric state of 3-phosphoglyceroyl-D-glyceraldehyde-3-phosphate dehydrogenase

M. Vas, S. Lakatos, J. Hajdu, P. Friedrich

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The specific activity of pig muscle d-glyceraldehyde-3-phosphate dehydrogenase was found to be constant in the reverse reaction, with NADH and 1,3-diphosphoglycerate as substrates, over the enzyme concentration range 10-8 to 10-4 M. The molecular weight of the covalent intermediate of the enzyme, 3-phosphoglyceroyl-glyceraldehyde-3-phosphate dehydrogenase, as measured by sedimentation techniques, proved constant (145 000 ± 6 000) between 3 × 10-7 and 3 × 10-5 M enzyme concentration. Likewise, no change in the apparent molecular weight was observed by gelcentration. The data indicate that the enzyme functions in its tetrameric form.

Original languageEnglish
Pages (from-to)89-96
Number of pages8
JournalBiochimie
Volume63
Issue number2
DOIs
Publication statusPublished - Feb 15 1981

ASJC Scopus subject areas

  • Biochemistry

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