Studies on Crystalline Yeast Phosphoglyceric Acid Mutase

1 January 1960

journal article
Published by Oxford University Press (OUP) in Bulletin of the Agricultural Chemical Society of Japan

Vol. 24 (6) , 555-557
https://doi.org/10.1271/bbb1924.24.555

Abstract

The apparent Michaelis constants of each component for the coenzyme are the same values. Each component is inhibited by the substrate according to the same mechanism. The optimal pH values and the equilibrium constants of the reactions catalyzed by each component are the same. E^1%_1cm (280mμ) values of each component are are identical. E_280mμ/E_260mμ absorption ratios also similar. It may be concluded that each component is almost the same enzyme protein.

Keywords

PROTEIN
OPTIMAL
PH VALUES
EQUILIBRIUM CONSTANTS
REACTIONS CATALYZED
MICHAELIS CONSTANTS
ACID MUTASE
CRYSTALLINE YEAST
APPARENT MICHAELIS
E280MΜ/E260MΜ ABSORPTION

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