Author:
Seargeant L E,Stinson R A
Abstract
Orthovanadate was shown to be a potent competitive inhibitor (Ki less than 1 microM) of purified alkaline phosphatase from human liver, intestine of kidney. Inhibition was reversed and full enzymic activity restored in the presence of 1mM-adrenaline. Phosphate and vanadate competed for the same binding site on the enzyme.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
105 articles.
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