The Use of an All-or-None Assay for Measuring Enzyme-activator Dissociation Constants

The rate at which Mg 2+ dissociates from the catalytically active magnesium-enzyme-substrate complex is much smaller than the catalytic rate in the phosphoglucomutase system. This observation was used in designing an all-or-none type of assay to distinguish between the free enzyme and its Mg 2+ comp...

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Bibliographic Details
Published in:The Journal of biological chemistry 1966-02, Vol.241 (4), p.1012-1015
Main Authors: Ray, Jr, W J, Roscelli, G A
Format: Article
Language:English
Subjects:
Catalysis
Chemical Phenomena
Chemistry
Hexosephosphates
Kinetics
Magnesium
Phosphoglucomutase
Zinc
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Summary:The rate at which Mg 2+ dissociates from the catalytically active magnesium-enzyme-substrate complex is much smaller than the catalytic rate in the phosphoglucomutase system. This observation was used in designing an all-or-none type of assay to distinguish between the free enzyme and its Mg 2+ complex, and hence to measure the dissociation constant for the Mg 2+ complex of phosphoglucomutase.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)96866-3