Please use this identifier to cite or link to this item:
|Title:||Characterization of a tissue kallikrein inhibitor isolated from Bauhinia bauhinioides seeds: inhibition of the hydrolysis of kininogen related substrates|
Mendes, C. R.
Juliano, M. A.
Rosa, J. C.
Greene, L. J.
Sampaio, M. U.
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
serine proteinase inhibitor
blood clotting enzymes
tissue kallikrein inhibitor
|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.|
|Appears in Collections:||Artigo|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.