Lentil seedling amine oxidase: interaction with carbonyl reagents.

Abstract

Carbonyl reagents containing a primary amino group were covalently bound by lentil seedling amine oxidase to resolve conflicting data for both the number of functional active sites in the dimeric enzyme. Active site titration of highly purified enzyme samples with all the carbonyl reagents extrapolates to 1 mol of inhibitor/mol of enzyme subunit indicating… (More)

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