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Title: Characterization of a tissue kallikrein inhibitor isolated from Bauhinia bauhinioides seeds: inhibition of the hydrolysis of kininogen related substrates
Authors: Oliva, MLV
Mendes, C. R.
Juliano, M. A.
Chagas, JR
Rosa, J. C.
Greene, L. J.
Sampaio, M. U.
Sampaio, CAM
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Keywords: kallikrein
serine proteinase inhibitor
blood clotting enzymes
tissue kallikrein inhibitor
Issue Date: 1-Dec-1999
Publisher: Elsevier B.V.
Citation: Immunopharmacology. Amsterdam: Elsevier B.V., v. 45, n. 1-3, p. 163-169, 1999.
Abstract: Trypsin inhibitors were purified from a saline extract of Bauhinia bauhinioides seeds by ion-exchange column chromatography on DEAE-Sephadex, gel filtration on Superose 12 column, Mono Q ion-exchange chromatography or, alternatively, by affinity chromatography on trypsin-Sepharose. Both B. bauhinioides isolated inhibitors, BbTI-I and BbTI-II, inhibit trypsin being the dissociation constant 0.6 and 0.36 nM, respectively. BbTI-II only inhibits porcine pancreatic kallikrein hydrolysis of H-Pro-Phe-Arg-AMC (K-i 2.0 nM); the bradykinin-containing sequence LGMISLMKRPPGFSPFRSSRI-NH2 and the two kininogen related flanking quenched substrates Abz-MISLMKRP-EDDnp (K-i 2.0 nM) and Abz-FRSSRQ-EDDnp (K-i 2.5 nM). (C) 1999 Published by Elsevier Science B.V. All rights reserved.
ISSN: 0162-3109
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