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Interaction between glyceraldehyde-3-phosphate-dehydrogenase and lactate dehydrogenase.

Authors
  • Sukhodolets, M V
  • Muronetz, V I
  • Nagradova, N K
Type
Published Article
Journal
Biochemistry international
Publication Date
Aug 01, 1989
Volume
19
Issue
2
Pages
379–384
Identifiers
PMID: 2818602
Source
Medline
License
Unknown

Abstract

Physical interaction between rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase was detected by means of matrix immobilization technique. Glyceraldehyde-3-phosphate dehydrogenase covalently bound to CNBr-activated Sepharose 4B was capable of forming a complex with soluble lactate dehydrogenase with a stoichiometry of 0.8 mole of lactate dehydrogenase per mole of glyceraldehyde-3-phosphate dehydrogenase and KD of 0.385 microM at pH 6.5. The bienzyme association weakened when pH changed to 7.0 (the KD increased to 1.25 microM).

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