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Interaction between glyceraldehyde-3-phosphate-dehydrogenase and lactate dehydrogenase
M V Sukhodolets1, V I Muronetz, N K Nagradova
1A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Biochemistry International
|August 1, 1989
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).