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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleThe complete amino acid sequence of a trypsin inhibitor from Bauhinia variegata var. candida seedspt_BR
dc.contributor.authorDi Ciero, Lpt_BR
dc.contributor.authorOliva, MLVpt_BR
dc.contributor.authorTorquato, Rpt_BR
dc.contributor.authorKohler, Ppt_BR
dc.contributor.authorWeder, JKPpt_BR
dc.contributor.authorNovello, JCpt_BR
dc.contributor.authorSampaio, CAMpt_BR
dc.contributor.authorOliveira, Bpt_BR
dc.contributor.authorMarangoni, Spt_BR
unicamp.authorUNIFESP, Escola Paulista Med, Dept Biochem, BR-04044900 Sao Paulo, Brazil Tech Univ Munich, Inst Lebensmittelchem, D-85748 Garching, Germany Deutsch Forsch Anstalt Lebensmittelchem, D-85748 Garching, Germany Univ Estadual Campinas, Inst Biol, Dept Biochem, BR-13083970 Campinas, SP, Brazilpt_BR
dc.subjecttrypsin inhibitorpt_BR
dc.subjectBauhinia variegata seedspt_BR
dc.subjectprimary structurept_BR
dc.subjectsequence homologypt_BR
dc.description.abstractTrypsin inhibitors of two varieties of Bauhinia variegata seeds have been isolated and characterized. Bauhinia variegata candida trypsin inhibitor (BvcTI) and B. variegata lilac trypsin inhibitor (BVlTI) are proteins with M-r of about 20,000 without free sulfhydryl groups. Amino acid analysis shows a high content of aspartic acid, glutamic acid, serine, and glycine, and a low content of histidine, tyrosine, methionine, and lysine in both inhibitors. Isoelectric focusing for both varieties detected three isoforms (pI 4.85, 5.00, and 5.15), which were resolved by HPLC procedure. The trypsin inhibitors show K-i values of 6.9 and 1.2 nM for BvcTI and BvlTI, respectively. The N-terminal sequences of the three trypsin inhibitor isoforms from both varieties of Bauhinia variegata and the complete amino acid sequence of B. variegata var. candida L. trypsin inhibitor isoform 3 (BvcTI-3) are presented. The sequences have been determined by automated Edman degradation of the reduced and carboxymethylated proteins of the peptides resulting from Staphylococcus aureus protease and trypsin digestion. BvcTI-3 is composed of 167 residues and has a calculated molecular mass of 18,529. Homology studies with other trypsin inhibitors show that BvcTI-3 belongs to the Kunitz family. The putative active site encompasses Arg (63)-Ile (64).pt
dc.relation.ispartofJournal Of Protein Chemistrypt_BR
dc.relation.ispartofabbreviationJ. Protein Chem.pt_BR
dc.publisher.cityNew Yorkpt_BR
dc.publisherKluwer Academic/plenum Publpt_BR
dc.identifier.citationJournal Of Protein Chemistry. Kluwer Academic/plenum Publ, v. 17, n. 8, n. 827, n. 834, 1998.pt_BR
dc.sourceWeb of Sciencept_BR
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dc.description.provenanceMade available in DSpace on 2015-11-26T16:18:01Z (GMT). No. of bitstreams: 2 WOS000078226100011.pdf: 773789 bytes, checksum: 5d2a678e99cb4c0bd6ec652b0bce1bb4 (MD5) WOS000078226100011.pdf.txt: 22826 bytes, checksum: 04c0239b481bb334c517ce7c176ffab9 (MD5) Previous issue date: 1998en
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