ABSTRACT
Limited and extensive proteolysis occur when ß-conglycinin ß homo-trimer (ß(3)-conglycinin) from soybeans is attacked by papain. Slow limited proteolysis is restricted to cleavage of ß(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. In contrast, limited proteolysis of phaseolin from common beans has been found to be prerequisite for the onset of its extensive proteolysis. The dramatic distinction between the degradation patterns of ß(3)-conglycinin and phaseolin, homologous storage 7S globulins, suggests the existence of intrinsic differences in their structures. This hypothesis is supported by comparative analysis of the accessibilities to the solvent of amino acid residues in phaseolin and ß(3)-conglycinin structures, which indicated the relatively low packing density of the latter, resulting in enhanced susceptibility of it to extensive proteolysis.
Subject(s)
Antigens, Plant/chemistry , Antigens, Plant/metabolism , Globulins/chemistry , Globulins/metabolism , Papain/metabolism , Protein Multimerization , Proteolysis , Seed Storage Proteins/chemistry , Seed Storage Proteins/metabolism , Soybean Proteins/chemistry , Soybean Proteins/metabolism , Amino Acid Sequence , Hydrolysis , Kinetics , Models, Molecular , Molecular Sequence Data , Molecular Weight , Peptide Fragments/chemistry , Peptide Fragments/metabolism , Protein Structure, Quaternary , Glycine max , Substrate SpecificityABSTRACT
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.
