Characterization of a tissue kallikrein inhibitor isolated from Bauhinia bauhinioides seeds: inhibition of the hydrolysis of kininogen related substrates
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1999-12-01
Autores
Oliva, MLV
Mendes, C. R.
Juliano, M. A.
Chagas, JR
Rosa, J. C.
Greene, L. J.
Sampaio, M. U.
Sampaio, CAM
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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.
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Immunopharmacology. Amsterdam: Elsevier B.V., v. 45, n. 1-3, p. 163-169, 1999.