Primary structure of a Kunitz-type trypsin inhibitor from Enterolobium contortisiliquum seeds

Primary structure of a Kunitz-type trypsin inhibitor from Enterolobium contortisiliquum seeds

Autor Batista, IFC Google Scholar
Oliva, MLV Google Scholar
Araujo, M. S. Google Scholar
Sampaio, M. U. Google Scholar
Richardson, M. Google Scholar
Fritz, H. Google Scholar
Sampaio, CAM Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
UNIV DURHAM
UNIV MUNICH
Resumo A trypsin inhibitor was isolated from Enterolobium contortisiliquum seeds. Starting with a saline extract, ECTI (E. contortisiliquum trypsin inhibitor) was purified as a homogeneous protein by acetone precipitation, ion-exchange chromatography (DEAE-Sephadex A-50), gel filtration (Sephadex G-75 and Superose 12) and reversed phase HPLC (mu-Bondapak C-18). the amino acid sequence was determined by automatic degradation and by DABITC/PITC microsequence analysis of the reduced and carboxymethylated protein and also of purified peptides derived from the protein by cleavage with iodosobenzoic acid and by enzymic digestion with trypsin, chymotrypsin and Staphylococcus aureus V8 protease. ECTI contains 174 amino acid residues in two polypeptide chains, an cc-chain consisting of 134 residues and a beta-chain made up of 40 residues. the inhibitor displays a high degree of sequence identity with other Kunitz-type proteinase inhibitors isolated from the Mimosoideae subfamily. the reactive site was identified (by homology) as the arginine-isoleucine peptide bond at position 64-65. ECTI inhibits trypsin and chymotrypsin in the stoichiometric ratio of 1:1 and also Factor XIIa, plasma kallikrein and plasmin, but not thrombin and Factor Xa.
Palavra-chave Enterolobium contortisiliquum
Leguminosae
Mimosoideae
seeds
serine proteinase inhibitor
amino acid sequence
blood dotting enzymes
Idioma Inglês
Data de publicação 1996-03-01
Publicado em Phytochemistry. Oxford: Pergamon-Elsevier B.V., v. 41, n. 4, p. 1017-1022, 1996.
ISSN 0031-9422 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 1017-1022
Fonte http://dx.doi.org/10.1016/0031-9422(95)00710-5
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1996TX84700003
Endereço permanente http://repositorio.unifesp.br/handle/11600/25561

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