Authors: L G Mezhlumyan M A Kuchenkova P Kh Yuldashev
Publish Date: 1986/11/01
Volume: 22, Issue: 6, Pages: 686-689
Abstract
Protease A has been isolated in the homogeneous state from dormant seeds of cotton plants of the TashkentI variety A scheme is proposed for the isolation and purification of the enzyme which includes the following stages extraction of the defatted seeds with 01 M phosphate buffer pH 74 precipitation of the protein with ammonium sulfate at 60 saturation desalting by dialysis and ionexchange chromatography on a column containing CM and DEAEcelluloses The molecular weight of the enzyme has been determined as 60000 The enzyme efficiently hydrolyzes azocasein and the 7S and 11S reserve proteins of cotton seeds Its maximum activity appears at pH 64–74 and a temperature of 35–40°C it is not activated by sulfhydryl reagents and loses its activity in the presence of diisopropyl phosphorofluoridate The assumption is made that protease A belongs to the serine type of trypsinlike proteases
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