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Characterization of wheat o-diphenolase isoenzyme
Authors:Francesco S Interesse  Pacifico Ruggiero  Gerolmina D&#x;Avella  Francesco Lamparelli
Institution:1. Istituto di Chimica Agraria, Universitá degli Studi di Bari, Via Amendola 165/a, 70126, Bari, Italy
Abstract:A highly purified isoenzyme of wheat o-diphenolase was characterized. The isoenzyme had a MW of ca 115 000, as determined by Sephadex G-100 gel filtration. The copper content was 0.20%, and the amino acid composition was determined. Two subunits (MWs ca 30 000 and 23 500) were detected by SDS gel electrophoresis. The Km was found to be 5.1 mM for 4-methylcatechol and kinetic analysis showed that the isoenzyme exhibited substrate inhibition. The isoenzyme was characterized by its response to some inhibitors.
Keywords:Gramineae  wheat  isoenzyme  MW  copper content  amino acid composition  kinetic properties  inhibitors  
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