Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/195017
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
Fabaceae
Molecular Sequence Data
Peptides
Plant Proteins
Plants, Medicinal
Seeds
Sequence Homology, Amino Acid
Trypsin Inhibitors
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/11397427
Date Issue: 2001
Appears in Collections:Unicamp - Artigos e Outros Documentos

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