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Wilson KA, Rightmire BR, Chen JC, et al. Differential Proteolysis of Glycinin and beta-Conglycinin Polypeptides during Soybean Germination and Seedling Growth. Plant Physiol. 1986;82(1):71-6doi: 10.1104/pp.82.1.71.
Wilson, K. A., Rightmire, B. R., Chen, J. C., & Tan-Wilson, A. L. (1986). Differential Proteolysis of Glycinin and beta-Conglycinin Polypeptides during Soybean Germination and Seedling Growth. Plant physiology, 82(1), 71-6. https://doi.org/10.1104/pp.82.1.71
Wilson, K A, et al. "Differential Proteolysis of Glycinin and beta-Conglycinin Polypeptides during Soybean Germination and Seedling Growth." Plant physiology vol. 82,1 (1986): 71-6. doi: https://doi.org/10.1104/pp.82.1.71
Wilson KA, Rightmire BR, Chen JC, Tan-Wilson AL. Differential Proteolysis of Glycinin and beta-Conglycinin Polypeptides during Soybean Germination and Seedling Growth. Plant Physiol. 1986 Sep;82(1):71-6. doi: 10.1104/pp.82.1.71. PMID: 16665026; PMCID: PMC1056068.
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Plant Physiol. 1986 Sep;82(1):71-6. doi: 10.1104/pp.82.1.71.

Differential Proteolysis of Glycinin and beta-Conglycinin Polypeptides during Soybean Germination and Seedling Growth.

Plant physiology

K A Wilson, B R Rightmire, J C Chen, A L Tan-Wilson

Affiliations

  1. Department of Biological Sciences, State University of New York at Binghamton, Binghamton, New York 13901.

PMID: 16665026 PMCID: PMC1056068 DOI: 10.1104/pp.82.1.71

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 beta-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 beta-conglycinin specific antibodies. The three subunits of beta-conglycinin were preferentially metabolized. Of the three subunits of beta-conglycinin, the larger alpha and alpha' subunits are rapidly degraded, generating new beta-conglycinin cross-reactive polypeptides of 51,200 molecular weight soon after imbibition of the seed. After 6 days of growth the beta-subunit is also hydrolyzed. At least six polypeptides, ranging from 33,100 to 24,000 molecular weight, appear as apparent degradation products of beta-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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