Abstract
The degradation of the major seed storage globulins of the soybean (Glycine max [L.] Merrill) was examined during the first 12 days of germination and seedling growth. The appearance of glycinin and β-conglycinin degradation products was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of cotyledon extracts followed by electroblotting to nitrocellulose and immunostaining using glycinin and β-conglycinin specific antibodies. The three subunits of β-conglycinin were preferentially metabolized. Of the three subunits of β-conglycinin, the larger α and α′ subunits are rapidly degraded, generating new β-conglycinin cross-reactive polypeptides of 51,200 molecular weight soon after imbibition of the seed. After 6 days of growth the β-subunit is also hydrolyzed. At least six polypeptides, ranging from 33,100 to 24,000 molecular weight, appear as apparent degradation products of β-conglycinin. The metabolism of the glycinin acidic chains begins early in growth. The glycinin acidic chains present at day 3 have already been altered from the native form in the ungerminated seed, as evidenced by their higher mobility in an alkaline-urea polyacrylamide gel electrophoresis system. However, no change in the molecular weight of these chains is detectable by sodium dodecyl sulfate-polyarylamide gel electrophoresis. Examination of the glycinin polypeptide amino-termini by dansylation suggests that this initial modification of the acidic chains involves limited proteolysis at the carboxyl-termini, deamidation, or both. After 3 days of growth the acidic chains are rapidly hydrolyzed to a smaller (21,900 molecular weight) form. The basic polypeptides of glycinin appear to be unaltered during the first 8 days of growth, but are rapidly degraded thereafter to unidentified products. All of the original glycinin basic chains have been destroyed by day 10 of growth.
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- Bond H. M., Bowles D. J. Characterization of soybean endopeptidase activity using exogenous and endogenous substrates. Plant Physiol. 1983 Jun;72(2):345–350. doi: 10.1104/pp.72.2.345. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Catsimpoolas N., Campbell T. G., Meyer E. W. Immunochemical study of changes in reserve proteins of germinating soybean seeds. Plant Physiol. 1968 May;43(5):799–805. doi: 10.1104/pp.43.5.799. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Harboe N., Ingild A. Immunization, isolation of immunoglobulins, estimation of antibody titre. Scand J Immunol Suppl. 1973;1:161–164. doi: 10.1111/j.1365-3083.1973.tb03798.x. [DOI] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Moreira M. A., Hermodson M. A., Larkins B. A., Nielsen N. C. Partial characterization of the acidic and basic polypeptides of glycinin. J Biol Chem. 1979 Oct 10;254(19):9921–9926. [PubMed] [Google Scholar]
- Shutov A. D., Do N. L., Vaintraub I. A. Ochistka i chastichnaia kharakteristika proteazy B iz prorastaiushchikh semian viki. Biokhimiia. 1982 May;47(5):814–821. [PubMed] [Google Scholar]
- Staswick P. E., Nielsen N. C. Characterization of a soybean cultivar lacking certain glycinin subunits. Arch Biochem Biophys. 1983 May;223(1):1–8. doi: 10.1016/0003-9861(83)90565-9. [DOI] [PubMed] [Google Scholar]
- Tan-Wilson A. L., Rightmire B. R., Wilson K. A. Different Rates of Metabolism of Soybean Proteinase Inhibitors during Germination. Plant Physiol. 1982 Aug;70(2):493–497. doi: 10.1104/pp.70.2.493. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Thanh V. H., Shibasaki K. Beta-conglycinin from soybean proteins. Isolation and immunological and physicochemical properties of the monomeric forms. Biochim Biophys Acta. 1977 Feb 22;490(2):370–384. doi: 10.1016/0005-2795(77)90012-5. [DOI] [PubMed] [Google Scholar]
- Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]