Immobilized glyceraldehyde-3-phosphate dehydrogenase forms a complex with phosphoglycerate kinase.
Yeast glyceraldehyde-3-phosphate dehydrogenase (GPDH) covalently attached to CNBr- activated Sepharose 4B was shown to be capable of binding soluble yeast phosphoglycerate kinase (PGK) in the course of incubation in the presence of an excess of 1,3-diphosphoglycerate. The association of the matrix-bound and soluble enzymes also occurred if the kinase was added to a reaction mixture in which the immobilized glyceraldehyde-3-phosphate dehydrogenase, NAD, glyceraldehyde-3-phosphate and Pi had been preincubated. Three kinase molecules were bound per a tetramer of the immobilized dehydrogenase and one molecule per a dimer. An immobilized monomer of glyceraldehyde-3-phosphate dehydrogenase was incapable of binding phosphoglycerate kinase. The matrix-bound bienzyme complexes were stable enough to survive extensive washings with a buffer and could be used repeatedly for activity determinations. Experimental evidence is presented to support the conclusion that 1,3-diphosphoglycerate produced by the kinase bound in a complex can dissociate into solution and be utilized by the dehydrogenase free of phosphoglycerate kinase.[1]References
- Immobilized glyceraldehyde-3-phosphate dehydrogenase forms a complex with phosphoglycerate kinase. Ashmarina, L.I., Muronetz, V.I., Nagradova, N.K. Biochem. Int. (1984) [Pubmed]
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