half cystine/phaseolus

A method is presented for the isolation of a lectin from a Brazilian cultivar of the common bean (Phaseolus vulgaris L.), through extraction in acidic (pH 4.2) medium, fractionation with ammonium sulfate, and chromatography on DEAE-cellulose. The lectin was shown to be homogeneous by gel

Four isoinhibitors against bovine pancreatic trypsin were purified from Phaseolus vulgaris(cv. Tora-mame) seeds by extraction with water(pH 2.0), ammonium sulfate fractionation, gel chromatography on Sephacryl S-200, trypsin-Sepharose gel affinity chromatography, and chromatofocusing. They inhibit

Treatment of raw soy flour with L-cysteine or N-acetyl-L-cysteine results in the introduction of new half-cystine residues into sulfur-poor legume proteins, with a corresponding improvement in nutritional quality as measured by the protein efficiency ratio (PER) in rats. The proteins are modified

Two proteinase inhibitors, designated as inhibitors I and II, were purified from adzuki beans (Phaseolus angularis) by chromatographies on DEAE- and CM-cellulose, and gel filtration on a Sephadex G-100 column. Each inhibitor shows unique inhibitory activities. Inhibitor I was a powerful inhibitor of

Two isoinhibitors (II and III-B) have been isolated from kidney bean (Phaseolus vulgaris L.) in a highly purified state. Both were active against trypsin and chymotrypsin to the same extent. Their amino acid composition is characterized by a high content of half-cystine, aspartic acid (or