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Cereal Chem 44:631 - 637.  |  VIEW ARTICLE
Purification and Structural Studies of the 11S Component of Soybean Proteins.

N. Catsimpoolas, D. A. Rogers, S. J. Circle, and E. W. Meyer. Copyright 1967 by the American Association of Cereal Chemists, Inc. 

Soybean globulins were separated into at least 12 components by disc electrophoresis on polyacrylamide gel. The 11S component of the cold-precipitated globulins was purified by ammonium sulfate precipitation followed by DEAE-Sephadex column chromatography. The 11S protein was dissociated by 6M guanidine hydrochloride containing 0.2M mercaptoethanol into at least 12 subunits. Quantitative N-terminal amino acid analysis of the 11S component indicated that the protein contains at least twelve polypeptide chains, eight of which end in glycine, two in phenylalanine, and two in either leucine or isoleucine. Amino acid analysis showed that several of the essential amino acids exhibit lower values in the 11S protein than in the whole soybean globulin fraction.

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