Subunit interaction in mammalian aldolases

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Subunit interaction in mammalian aldolases.

Enzyme inactivation was utilized to study subunit interaction in the homotetrameric glycolytic enzyme, aldolase. Isoenzymes from rabbit liver and skeletal muscle were inactivated in the presence of Pi and d-glyceraldehyde-P to a maximum stoichiometry of one modification per aldolase subunit. Subunit modification increased net negative charge on each subunit surface and was used to resolve modif...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1997

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3230671