Primary sequence determination of a Kunitz inhibitor isolated from Delonix regia seeds

Primary sequence determination of a Kunitz inhibitor isolated from Delonix regia seeds

Autor Pando, S. C. Google Scholar
Oliva, MLV Google Scholar
Sampaio, CAM Google Scholar
Di Ciero, L. Google Scholar
Novello, J. C. Google Scholar
Marangoni, S. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Universidade Estadual de Campinas (UNICAMP)
Resumo A serine proteinase inhibitor was purified from Delonix regia seeds a Leguminosae tree of the Caesalpinioideae subfamily. the inhibitor named DrTI, inactivated trypsin and human plasma kallikrein with K-i values 2.19x10(-8) M and 5.25 nM, respectively. Its analysis by SDS-PAGE 10-20% showed that the inhibitor is a protein with a single polypeptide chain of M-r 22 h Da. the primary sequence of the inhibitor was determined by Edman degradation, thus indicating that it contained 185 amino acids and showed that it belongs to the Kunitz type family; however, its reactive site did not contain Arg or Lys at the putative reactive site (position 63, SbTI numbering) or it was displaced when compared to other Kunitz-type inhibitors. (C) 2001 Elsevier B.V. All rights reserved.
Palavra-chave Delonix regia
Leguminosae
Kunitz inhibitor
serine proteinase
trypsin
human plasma kallikrein
Idioma Inglês
Data de publicação 2001-07-01
Publicado em Phytochemistry. Oxford: Pergamon-Elsevier B.V., v. 57, n. 5, p. 625-631, 2001.
ISSN 0031-9422 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 625-631
Fonte http://dx.doi.org/10.1016/S0031-9422(01)00080-2
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000169481100002
Endereço permanente http://repositorio.unifesp.br/handle/11600/26589

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