Open AccessAction of trypsin on glycinin
Author(s) -
SHUTOV Andrei D.,
PINEDA Julio,
SENYUK Vitalyi I.,
REVA Vyacheslav A.,
VAINTRAUB Iosif A.
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb16152.x
Subject(s) - proteolysis , chemistry , trypsin , molecular mass , hydrolysis , gel electrophoresis , chromatography , kinetics , biochemistry , enzyme , physics , quantum mechanics
The formation of a relatively stable high‐molecular‐mass product on trypsin hydrolysis of glycinin (glycinin‐T) is interpreted to be a result of ‘zipper’ proteolysis. Evidence of parallel one‐by‐one degradation of glycinin occurring after the formation of glycinin‐T is presented. At a relatively low concentration of the substrate, the one‐by‐one proteolysis proceeds as a first‐order reaction. A method of determination of the changes in the molecular mass of a protein during the mixed‐type proteolysis and some other parameters of this process is developed on the basis of the analysis of the proteolysis kinetics. The value of the molecular mass of glycinin‐T calculated by means of this method makes up 70% of the initial molecular mass and coincides with the result of direct determination by gradient gel electrophoresis.