Please use this identifier to cite or link to this item:
Type: Artigo de periódico
Title: Primary Sequence Determination Of A Kunitz Inhibitor Isolated From Delonix Regia Seeds.
Author: Pando, S C
Oliva, M L
Sampaio, C A
Di Ciero, L
Novello, J C
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.
Subject: Amino Acid Sequence
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
Molecular Sequence Data
Plant Proteins
Plants, Medicinal
Sequence Homology, Amino Acid
Trypsin Inhibitors
Citation: Phytochemistry. v. 57, n. 5, p. 625-31, 2001-Jul.
Rights: fechado
Date Issue: 2001
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File SizeFormat 
pmed_11397427.pdf458.62 kBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.