Abstract
Globulin proteins were isolated from a 0.5M NaCl extract of tartary buckwheat, then separated by column chromatography on Sephacryl S-300 and polyacrylamide gel electrophoresis. The results Showed that the tartary buckwheat globulins contained two kinds of globulin, with molecular weights of 679, 000 and 443, 000, respectively. Quantitatively, the latter was the major tartary buckwheat globulin. This major globulin had several bands on SDS-PAGE, which appeared as a single peak with a molecular weight of 178, 600 on gel filtration with 6M guanidine hydrochoride. These results provide evidence that the major globulin from tartary buckwheat is composed of two or three polypeptides, each with a molecular weight 178, 600, and linked with hydrogen bonds.
