Substrate-induced dissociation of glyceraldehyde-phosphate dehydrogenase detected by affinity chromatography. Study of subunit interactions by affinity sorption
- 1 August 1980
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Enzymology
- Vol. 614 (2), 285-293
- https://doi.org/10.1016/0005-2744(80)90218-1
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Quantitative uses of affinity chromatographyAnalytical Biochemistry, 1979
- Multiple binding sites of carboxypeptidase B: the evaluation of dissociation constants by quantitative affinity chromatographyBiochemistry, 1979
- Enzyme-enzyme interaction and the biosynthesis of aromatic amino acids in Escherichia coliBiochimica et Biophysica Acta (BBA) - Enzymology, 1979
- Use of blue dextran as a probe for the Nicotinamide Adenine Dinucleotide domain in proteinsAccounts of Chemical Research, 1977
- Evaluation of equilibrium constants by affinity chromatographyBiochemical Journal, 1974
- Theory of affinity chromatography separationsAnalytical Chemistry, 1974
- Effect of heavy water and nicotinamide adenine dinucleotide on the sedimentation properties and structure of glyceraldehyde phosphate dehydrogenaseBiochemistry, 1973
- Dissociation of mammalian D‐glyceraldehyde‐3‐phosphate dehydrogenase into monomersFEBS Letters, 1972
- Influence of substrates on the dissociation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenaseBiochemistry, 1969
- Glyceraldehyde 3-Phosphate Dehydrogenase from Pig MuscleNature, 1968