The action of pepsin on the reserve proteins of some leguminous seeds.
作者： I. A. Vaintraub , P. Seliger , A. D. Shutov
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摘要: The action of pepsin on the 11-S and 7-S proteins vetch, protein soybean Phaseolus vulgaris was investigated. first three are hydrolyzed almost completely, rate hydrolysis being close to that hemoglobin, while Ph. stops after cleavage only 2,4% peptide bonds. nonhydrolyzable high molecular weight core makes up 87% initial differs from latter in its electrophoretic mobility sedimentation coefficient. does not increase digestibility by trypsin. After consecutive these enzymes about two thirds remain unhydrolyzed. digestion is completed denaturation heat treatment or 6 M guanidine hydrochloride.
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