Identification of soybean glycinin precursor in vivo
1989
Kim, C.H. | Choi, Y.D. (Seoul National Univ., Suwon (Korea R.). Coll. of Agriculture)
Glycinin is the major storage protein in soybean. It has been known that a molecule of glycinin is composed of 6 subunits, each of which consists of two different kinds of polypeptides, acidic (A) and basic (B) one (MW 39K and 19K, respectively). To study the molecular origin and the relationship of glycinin subunit polypeptides, antibodies against A-and B-polypeptide were obtained by immunizing rabbits with either of the antigens purified by gel filtration and preparative electrophoresis. Each antibody was not only specific for its own antigen polypeptide in soybean but also recognized the precursor which was synthesized in vivo and in vitro. The polyadenylated mRNAs were isolated from immature seeds and leaves and were translated in vitro using wheat germ extract. One of the seed-specific translation products, MW 60K, was identified to be the precursor of glycinin subunit by immunoprecipitation with antibodies against glycinin A- and B-polypeptide. Mature A- and B-polypeptides were not detected in the translate in vitro. These results suggest that the precursor polypeptide is synthesized from the mRNA and is cleaved to yield A- and B-polypeptides which form a glycinin subunit in the cell. Glycinin genes were expressed with the maturation of soybean seeds in a tissue-specific and developmental stage-specific manner
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