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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 |
Citation: | Phytochemistry. v. 57, n. 5, p. 625-31, 2001-Jul. |
Rights: | fechado |
Address: | http://www.ncbi.nlm.nih.gov/pubmed/11397427 |
Date Issue: | 2001 |
Appears in Collections: | Unicamp - Artigos e Outros Documentos |
Files in This Item:
File | Size | Format | |
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pmed_11397427.pdf | 458.62 kB | Adobe PDF | View/Open |
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