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  • 1
    ISSN: 1573-4943
    Keywords: Trypsin inhibitor ; Kunitz-type inhibitor ; amino acid sequence ; winged bean ; Psophocarpus tetragonolobus (L.) DC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The primary sequence of trypsin inhibitor-2 (WBTI-2) fromPsophocarpus tetragonolobus (L.) DC seeds was determined. This inhibitor consists of a single polypeptide chain of 182 amino acids, including four half-cystine residues, and an N-terminal residue of pyroglutamic acid. The sequence of WBTI-2 showed 57% identity to the basic trypsin inhibitor (WBTI-3) and 50% identity to the chymotrypsin inhibitor (WBCI) of winged bean, and 54% identity to the trypsin inhibitor DE-3 fromErythrina latissima seed. The similarity to the soybean Kunitz trypsin inhibitor (40%) and the other Kunitz-type inhibitors fromAdenanthera pavonina (30%) and wheat (26%) was much lower. Sequence comparisons indicate that thePsophocarpus andErythrina inhibitors are more closely related to each other than to other members of the Kunitz inhibitor family.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4943
    Keywords: Trypsin inhibitor ; Kunitz-type seed inhibitor ; amino acid sequence ; sequence similarity ; Leguminosae ; winged bean ; Psophocarpus tetragonolobus (L.) DC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The primary structure of acidic trypsin inhibitor-2a (WBTI-2a,pI 5.9) fromPsophocarpus tetragonolobus (L.) DC seed was determined. This inhibitor consists of a single polypeptide chain of 180 amino acids including four half-cystine residues and has an N-terminal residue of pyroglutamic acid. The sequence of WBTI-2a,pI 5.9, showed 84% identity to acidic trypsin inhibitor-2 (WBTI-2,pI 5.1) but only 57% identity to the basic trypsin inhibitor (WBTI-1,pI 8.9) and 50% identity to the chymotrypsin inhibitor of winged bean. The data indicate that winged bean seed contains a family of three Kunitz-type inhibitors which have about 50% identity.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-9104
    Keywords: winged bean ; Psophocarpus tetragonolobus ; storage protein composition ; amino acid composition ; anti-nutritional factors ; proteinase inhibitors ; hemagglutinins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract The seeds of 27 varieties ofP. tetragonolobus from six regions of South-East Asia have been examined by polyacrylamide gel electrophoresis. No marked variations in the electrophoretic patterns were found which could be exploited by plant breeders to improve nutritional quality with respect to sulfur containing amino acids. The amino acid compositions of varieties from the different regions showed little variation. Seed extracts of all 27 varieties ofP. tetragonolobus showed trypsin and chymotrypsin inhibitory activities, and hemagglutinating activities. The levels of trypsin inhibitory activities showed some genotypic differences varying from 22.2 to 42.5 mg trypsin inbibited g−1 of seed meal. As a group the varieties from Malaysia showed the lowest levels of trypsin inhibitor. The chymotrypsin inhibitory activity also showed a similar variation (30.1–47.6 mg chymotrypsin inhibited g−1 of seed meal). Seed extracts agglutinated type O+ and B+ human and rabbit erythrocytes with little difference in activity between varieties. Autoclaving winged bean seed meal prior to protein extraction inactivated the anti-nutritional factors and resulted in considerable reduction of protein solubility.
    Type of Medium: Electronic Resource
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