The complete amino acid sequence of a trypsin inhibitor from Bauhinia variegata var. candida seeds

dc.creatorDi Ciero, L
dc.creatorOliva, MLV
dc.creatorTorquato, R
dc.creatorKohler, P
dc.creatorWeder, JKP
dc.creatorNovello, JC
dc.creatorSampaio, CAM
dc.creatorOliveira, B
dc.creatorMarangoni, S
dc.date1998
dc.dateNOV
dc.date2014-12-02T16:25:29Z
dc.date2015-11-26T16:18:01Z
dc.date2014-12-02T16:25:29Z
dc.date2015-11-26T16:18:01Z
dc.date.accessioned2018-03-28T23:01:54Z
dc.date.available2018-03-28T23:01:54Z
dc.identifierJournal Of Protein Chemistry. Kluwer Academic/plenum Publ, v. 17, n. 8, n. 827, n. 834, 1998.
dc.identifier0277-8033
dc.identifierWOS:000078226100011
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/74974
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/74974
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/74974
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1267571
dc.descriptionTrypsin 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).
dc.description17
dc.description8
dc.description827
dc.description834
dc.languageen
dc.publisherKluwer Academic/plenum Publ
dc.publisherNew York
dc.publisherEUA
dc.relationJournal Of Protein Chemistry
dc.relationJ. Protein Chem.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjecttrypsin inhibitor
dc.subjectBauhinia variegata seeds
dc.subjectprimary structure
dc.subjectsequence homology
dc.subjectProteinase-inhibitors
dc.subjectTityus-serrulatus
dc.subjectSerine-proteinase
dc.subjectKallikrein
dc.subjectEnzymes
dc.subjectPlants
dc.subjectToxin
dc.subjectVenom
dc.titleThe complete amino acid sequence of a trypsin inhibitor from Bauhinia variegata var. candida seeds
dc.typeArtículos de revistas


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