Action of trypsin on glycinin. Mixed-type proteolysis and its kinetics; molecular mass of glycinin-T.
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.
Shutov
A D
AD
Laboratory of Protein Chemistry, V.I. Lenin State University of Kishinev, USSR.
Pineda
J
J
Senyuk
V I
VI
Reva
V A
VA
Vaintraub
I A
IA
D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005916:Globulins / Q000302:isolation & purification / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D008433:Mathematics; D008970:Molecular Weight; D014674:Plant Proteins, Dietary / Q000378:metabolism; D030262:Soybean Proteins; D014357:Trypsin / Q000378:metabolism*
D005916:Globulins; D014674:Plant Proteins, Dietary; D030262:Soybean Proteins; C011474:glycinin; D014357:Trypsin