Human plasma kallikrein and tissue kallikrein binding to a substrate based on the reactive site of a factor Xa inhibitor isolated from Bauhinia ungulata seeds

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dc.contributor.authorOliva, MLV
dc.contributor.authorAndrade, S.
dc.contributor.authorBatista, IFC
dc.contributor.authorSampaio, M. U.
dc.contributor.authorJuliano, M.
dc.contributor.authorFritz, H.
dc.contributor.authorAuerswald, E. A.
dc.contributor.authorSampaio, CAM
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Munich
dc.date.accessioned2016-01-24T12:30:57Z
dc.date.available2016-01-24T12:30:57Z
dc.date.issued1999-12-01
dc.description.abstractKunitz type Bauhinia ungulata factor Xa inhibitor (BuXI) was purified from B. ungulata seeds. BuXI inactivates factor Xa and human plasma kallikrein (HuPK) with K-i values of 18.4 and 6.9 nM, respectively. However, Bauhinia variegata trypsin inhibitor (BvTI) which is 70% homologous to BuXI does not inhibit factor Xa and is less efficient on HuPK (K-i = 80 nM). the comparison between BuXI and BvTI reactive site structure indicates differences at Met(59), Thr(66) and Met(67) residues. the hydrolysis rate of quenched fluorescence peptide substrates based on BuXI reactive site sequence, Abz-VMIAALPRTMFIQ-EDDnp (leading peptide), by HuPK and porcine pancreatic kallikrein (PoPK) is low, but hydrolysis is enhanced with Abz-VMIAALPRTMQ-EDDnp, derived from the leading peptide shortened by removing the dipeptide Phe-Ileu from the C-terminal portion, for HuPK (K-m = 0.68 mu M, k(cat)/K-m = 1.3 X 10(6) M-1 s(-1)), and the shorter substrate Abz-LPRTMQ-EDDnp is better for PoPK (K-m = 0.66 mu M, k(cat)/K-m = 2.2 X 10(3) M-1 s(-1)). the contribution of substrate methionine residues to HuPK and PoPK hydrolysis differs from that observed with factor Xa. the determined K-m and k(cat) values suggest that the substrates interact with kallikreins the same as an enzyme and inhibitor interacts to form complexes. (C) 1999 Elsevier Science B.V. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv Munich, Chirurg Klin & Poliklin, Klin Chem & Klin Biochem Abt, Munich, Germany
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent145-149
dc.identifierhttp://dx.doi.org/10.1016/S0162-3109(99)00146-0
dc.identifier.citationImmunopharmacology. Amsterdam: Elsevier B.V., v. 45, n. 1-3, p. 145-149, 1999.
dc.identifier.doi10.1016/S0162-3109(99)00146-0
dc.identifier.issn0162-3109
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26192
dc.identifier.wosWOS:000084080100024
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofImmunopharmacology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjecthuman plasma kallikreinen
dc.subjecttissue kallikreinen
dc.subjectfactor Xaen
dc.subjectfluorogenic substratesen
dc.subjectserine proteinase inhibitoren
dc.subjectamino acid sequenceen
dc.subjectblood clotting enzymesen
dc.titleHuman plasma kallikrein and tissue kallikrein binding to a substrate based on the reactive site of a factor Xa inhibitor isolated from Bauhinia ungulata seedsen
dc.typeinfo:eu-repo/semantics/article
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