
Activation of Rabbit Muscle Phosphoglucomutase by Acid and Alkali
Author(s) -
Bocchini Vincenzo,
Najjar Victor A.
Publication year - 1970
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1970.tb00984.x
Subject(s) - chemistry , phosphoglucomutase , kinetics , cysteine , imidazole , alkali metal , enzyme , salt (chemistry) , biochemistry , inorganic chemistry , nuclear chemistry , organic chemistry , physics , quantum mechanics
Crystalline phosphoglucomutase can be activated almost two‐fold by preincubation in acid or alkali at optimal pH values of 3.5 and 10.5, respectively. The initial rate of such activation follows first order kinetics. Enzyme concentration affects the rate and extent of activation. This in turn is influenced by the salt concentration of the preincubation medium. Denaturation with loss of enzyme activity usually followed activation. However, stabilization of the activated state could be effected by imidazole, cysteine and EDTA in the presence of Mg 2+ . In the activated state there was no evidence of change in the molecular weight.