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- W2029129919 abstract "Tepary bean (Phaseolus acutifolius var. lactifolius) major storage globulin (>90% purity by electrophoresis) was composed of three glycosylated polypeptides with estimated molecular weights of 49 500, 45 890, and 44 510. The protein had an absorption maximum at 278 nm and an A1%280 nm of 6·61 in 20 mm Tris-HCI pH 8·1 containing 0·5 m NaCl. The carbohydrate content of the protein was 8·23% (w/w). The hydrodynamic radius (Stokes' radius) of the native protein was 53·3 A. Amino acid composition of the globulin indicated that S-containing amino acids were the first limiting amino acids. Acidic, basic, uncharged polar, and hydrophobic amino acids accounted for 28·75, 12·42, 21·94, and 36·91% (by weight), respectively of the total protein. The native globulin was resistant to in-vitro proteolysis. Heat denaturation (100°C, 30 min) of the globulin in aqueous 0·5 m NaCl did not improve the in-vitro proteolysis of the globulin. Heat denaturation (100°C, 30 min) of the globulin in the digestion buffer in the absence of NaCl facilitated complete in-vitro proteolysis of the globulin by chymotrypsin, trypsin, and pepsin." @default.
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- W2029129919 date "1994-01-01" @default.
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- W2029129919 title "Purification and biochemical characterization of tepary bean (Phaseolus acutifolius) major globulin" @default.
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