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Association of rabbit muscle glyceraldehyde‐3‐phosphate dehydrogenase and 3‐phosphoglycerate kinase The biochemical and electron‐microscopic evidence
Author(s) -
Sukhodolets Maks V.,
Muronetz Vladimir I.,
Tsuprun Valery L.,
Kaftanova Alla S.,
Nagradova Natalia K.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80248-5
Subject(s) - phosphoglycerate kinase , dehydrogenase , biochemistry , glyceraldehyde 3 phosphate dehydrogenase , enzyme , branched chain alpha keto acid dehydrogenase complex , chemistry , pyruvate dehydrogenase phosphatase , kinase , microbiology and biotechnology , biology , pyruvate dehydrogenase complex
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.
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