Purification and primary structure determination of a Bowman-Birk trypsin inhibitor from Torresea cearensis seeds

dc.creatorTanaka, AS
dc.creatorSampaio, MU
dc.creatorMarangoni, S
dc.creatordeOliveira, B
dc.creatorNovello, JC
dc.creatorOliva, MLV
dc.creatorFink, E
dc.creatorSampaio, CAM
dc.date1997
dc.dateMAR-APR
dc.date2014-07-30T14:18:42Z
dc.date2015-11-26T16:58:37Z
dc.date2014-07-30T14:18:42Z
dc.date2015-11-26T16:58:37Z
dc.date.accessioned2018-03-28T23:46:15Z
dc.date.available2018-03-28T23:46:15Z
dc.identifierBiological Chemistry. Walter De Gruyter & Co, v. 378, n. 41732, n. 273, n. 281, 1997.
dc.identifier1431-6730
dc.identifierWOS:A1997WZ88900021
dc.identifier10.1515/bchm.1997.378.3-4.273
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/58467
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/58467
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1277973
dc.descriptionA Bowman-Birk-type trypsin inhibitor (TcTl) was purified from seeds of Torresea cearensis, a Brazilian native tree of the Papilionoideae sub-family of Leguminosae, Three forms of the inhibitor were separated by an ion exchange ch ro matography, The major form with 63 amino acids was entirely sequenced; it shows a high structural similarity to the Bowman-Birk inhibitors from other Leguminosae, The putative reactive sites of the inhibitor are a lysine residue at position 15 and a histidine at position 42 as identified by alignment to related inhibitors, direct chemical modification and specific enzymatic degradation, Immunoprecipitation with antibodies raised in rats is reduced significantly if TcTl is complexed with chymotrypsin and, to a lesser degree, if complexed with trypsin, TcTl forms a ternary complex with trypsin and chymotrypsin, The binary complexes with trypsin or chymotrypsin were isolated by gel filtration. Dissociation constants of the complexes with trypsin, plasmin, chymotrypsin, and factor XIIa are 1,36, 50, 1450 nM, respectively; human plasma kallikrein, human factor Xa, porcine pancreatic kallikrein and bovine thrombin are not inhibited, TcTl prolongs blood clotting time of the contact phase activation pathway by inhibition of FXIIa.
dc.descriptiono TEXTO COMPLETO DESTE ARTIGO, ESTARÁ DISPONÍVEL À PARTIR DE AGOSTO DE 2015.
dc.description378
dc.description41732
dc.description273
dc.description281
dc.languageen
dc.publisherWalter De Gruyter & Co
dc.publisherBerlin
dc.publisherAlemanha
dc.relationBiological Chemistry
dc.relationBiol. Chem.
dc.rightsembargo
dc.sourceWeb of Science
dc.subjectblood clotting
dc.subjectchymotrypsin (EC 3.4.21.1)
dc.subjectfactor XII (EC 3.4.21.38)
dc.subjectplasmin (EC 3.4.21.7)
dc.subjectproteinase inhibitor
dc.subjectserine proteinases
dc.subjecttrypsin (EC 3.4.21.4)
dc.subjectAmino-acid-sequence
dc.subjectProteinase-inhibitor
dc.subjectChymotrypsin Inhibitor
dc.subjectSerine-proteinase
dc.subjectFamily
dc.subjectCleavage
dc.subjectLeaves
dc.subjectBeans
dc.subjectSites
dc.titlePurification and primary structure determination of a Bowman-Birk trypsin inhibitor from Torresea cearensis seeds
dc.typeArtículos de revistas


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