Association of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase The biochemical and electron-microscopic evidence

Maks V. Sukhodolets, Vladimir I. Muronetz, Valery L. Tsuprun, Alla S. Kaftanova, Natalia K. Nagradova

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble 3-phosphoglycerate kinase. The strength of the association appeared to depend upon the functional state of both enzymes. The holoform of the dehydrogenase exhibited a lower affinity for the kinase than the enzyme-3-phosphoglycerol·NADH complex. The substrate-free 3-phosphoglycerate kinase associated much stronger with the acylated dehydrogenase than the kinase in complex with 1,3-diphosphoglycerate. Electron-microscopic evidence for the association of the soluble acyl-glyceraldehyde-3-phosphate dehydrogenase·NADH complex and 3-phosphoglycerate kinase was also obtained.

Original languageEnglish (US)
Pages (from-to)161-166
Number of pages6
JournalFEBS Letters
Volume238
Issue number1
DOIs
StatePublished - Sep 26 1988

Keywords

  • 3-Phosphoglycerate kinase
  • Bienzyme complex
  • Electron-microscopic study
  • Glyceraldehyde-3-phosphate dehydrogenase

Fingerprint Dive into the research topics of 'Association of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase The biochemical and electron-microscopic evidence'. Together they form a unique fingerprint.

Cite this