Characterization of enzyme-enzyme interaction using an affinity batch system.

M Kálmán; L Boross

doi:10.1016/0167-4838(82)90156-x

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Characterization of enzyme-enzyme interaction using an affinity batch system.

M Kálmán·L Boross

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Abstract

NAD-Sepharose 4B gel was used to study the complexation between glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating) EC 1.2.1.12) and aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13). An affinity sorbent specific for glyceraldehyde-3-phosphate dehydrogenase was utilised in a batch system. The dissociation constant of the enzyme complex was calculated. The method elaborated in our laboratory was used to investigate the effects of temperature and pH on the complex formation.

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Chromatography, Affinity Fructose-Bisphosphate Aldolase Glyceraldehyde-3-Phosphate Dehydrogenases Hydrogen-Ion Concentration Kinetics Macromolecular Substances NAD Protein Binding Temperature Journal Article

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M Kálmán, L Boross. 1982-06-04. Characterization of enzyme-enzyme interaction using an affinity batch system.. https://doi.org/10.1016/0167-4838(82)90156-x

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