| Literature DB >> 4038299 |
Abstract
Molecular weights of native membrane-bound alkaline phosphatase released by butanol and by nonionic detergents were more than twice that of the purified dimeric enzyme. Alkaline phosphatase released by phosphatidylinositol-specific phospholipase-C was of both high and low molecular weight: the former was a protomer of a single protein of the same molecular size as monomeric alkaline phosphatase. We conclude that the membrane-bound enzyme is probably a tetramer.Entities:
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Year: 1985 PMID: 4038299 DOI: 10.1016/0006-291x(85)91806-6
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575