Degradation of β-conglycinin β-homotrimer by papain: independent occurrence of limited and extensive proteolysis.

Limited and extensive proteolysis occur when β-conglycinin β homo-trimer (β(3)-conglycinin) from soybeans is attacked by papain. Slow limited proteolysis is restricted to cleavage of β(3)-conglycinin polypeptides into subunit halves (N- and C-terminal domains) that are further slightly truncated. The kinetics of limited and extensive proteolyses analyzed separately indicates that the two processes occur independently from the very beginning of the reaction.

Soybean basic 7S globulin: subunit heterogeneity and molecular evolution.

Basic 7S globulin, a cysteine-rich protein from soybean seeds, consists of subunits containing 27 kD and 16 kD chains linked by disulfide bonding. Three differently sized subunits of the basic 7S globulin were detected and partially separated by SP Sepharose chromatography. The basic 7S globulin was characterized as a member of a superfamily of structurally related but functionally distinct proteins descended from a specific group of plant aspartic proteinases.