Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/58467
Type: Artigo de periódico
Title: Purification and primary structure determination of a Bowman-Birk trypsin inhibitor from Torresea cearensis seeds
Author: Tanaka, AS
Sampaio, MU
Marangoni, S
deOliveira, B
Novello, JC
Oliva, MLV
Fink, E
Sampaio, CAM
Abstract: A 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.
Subject: blood clotting
chymotrypsin (EC 3.4.21.1)
factor XII (EC 3.4.21.38)
plasmin (EC 3.4.21.7)
proteinase inhibitor
serine proteinases
trypsin (EC 3.4.21.4)
Country: Alemanha
Editor: Walter De Gruyter & Co
Rights: embargo
Identifier DOI: 10.1515/bchm.1997.378.3-4.273
Date Issue: 1997
Appears in Collections:Unicamp - Artigos e Outros Documentos

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