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psophocarpus/half cystine
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8 resultados
Purification and properties of the basic lectins from winged bean seed [Psophocarpus tetragonolobus (L.) DC].
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The seeds of winged bean, Psophocarpus tetragonolobus (L.) DC, contain a group of acidic lectins (pI approximately equal to 5.5) and a group of basic lectins (pI greater than 9.5) characterised by different erythrocyte hemagglutinating specificities. Three basic lectins were separated and purified
Characterization of the acidic lectins from winged bean seed (Psophocarpus tetragonolobus(L.)DC).
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The seeds of winged bean, Psophocarpus tetragonolobus(L.)DC, contain two distinct groups of lectins characterized by different erythrocyte hemagglutinating specificities and isoelectric points. Three acidic lectins (I, II, and III) (pI approximately 5.5) were purified to apparent homogeneity by
Amino acid sequence of the acidic Kunitz-type trypsin inhibitor from winged-bean seed [Psophocarpus tetragonolobus (L.) DC].
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The primary sequence of trypsin inhibitor-2 (WBTI-2) from Psophocarpus 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
Isolation and properties of a chymotrypsin inhibitor from winged bean seed (Psophocarpus tetragonolobus (L) Dc.).
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A new inhibitor of bovine alpha-chymotrypsin has been isolated from winged bean seed. The inhibitor was purified to homogeneity by affinity chromatography on chymotrypsin-Sepharose, following the removal of the trypsin inhibitors on trypsin-Sepharose. The inhibitor has a molecular weight of approx.
Isolation and characterization of the trypsin inhibitors from winged bean seed (Psophocarpus tetragonolobus (L) Dc.).
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The trypsin inhibitors from winged bean seed were isolated by affinity chromatography on trypsin-Sepharose 4B and the components fractionated by chromatography on SP-Sephadex C-25 and Sephadex G-100. The major components, inhibitors 2 and 3 were found to be homogeneous proteins with molecular
Primary structure of Kunitz-type trypsin inhibitor-2a (pI 5.9) from Psophocarpus tetragonolobus (L.) DC seed.
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The primary structure of acidic trypsin inhibitor-2a (WBTI-2a, pI 5.9) from Psophocarpus 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
Amino acid sequence and disulfide bridges of affinity purified Kunitz-type chymotrypsin inhibitor from winged bean seed (Psophocarpus tetragonolobus (L.) DC).
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The primary sequence of the affinity purified chymotrypsin inhibitor, WBCI, isolated from the albumin fraction of Psophocarpus tetragonolobus (L.) DC cv. UPS-122 seed was determined. The inhibitor consisted of a single polypeptide chain of 183 amino acids (Mr 20285) and the four half-cystine
Purification and characterization of proteinase inhibitors from winged bean (Psophocarpus tetragonolobus (L.) DC.) seeds.
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Seven proteinase inhibitors were isolated from winged bean seeds by ion-exchange chromatographies. These inhibitors had molecular weights of around 20,000, included four half-cystine residues, and were Kunitz-type inhibitors. Two (WTI-2 and 3) inhibited bovine trypsin strongly and four (WCI-1, 2, 3,
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