Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/70286
Type: Artigo de periódico
Title: Primary sequence determination of a Kunitz inhibitor isolated from Delonix regia seeds
Author: Pando, SC
Oliva, MLV
Sampaio, CAM
Di Ciero, L
Novello, JC
Marangoni, S
Abstract: 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 Science Ltd. All rights reserved.
Subject: Delonix regia
Leguminosae
Kunitz inhibitor
serine proteinase
trypsin
human plasma kallikrein
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/S0031-9422(01)00080-2
Date Issue: 2001
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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