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http://repositorio.unicamp.br/jspui/handle/REPOSIP/53944
Type: | Artigo de periódico |
Title: | A Trypsin Inhibitor from Sapindus saponaria L. Seeds: Purification, Characterization, and Activity Towards Pest Insect Digestive Enzyme |
Author: | Macedo, MLR Diz, EBS Freire, MGM Oliva, MLV Sumikawa, JT Toyama, MH Marangoni, S |
Abstract: | The present paper describes the purification, characterization and determination of the partial primary structure of the first trypsin inhibitor isolated from the family Sapindaceae. A highly stable, potent trypsin inhibitor (SSTI) was purified to homogeneity. SDS-PAGE analysis revealed that the protein consists of a two-polypeptide chain with molecular masses of approximately 15 and 3 kDa. The purified inhibitor inhibited bovine trypsin at a 1:1 M ratio. Kinetic analysis revealed that the protein is a competitive inhibitor with an equilibrium dissociation constant of 10(-9) M for trypsin. The partial NH(2)- terminal sequence of 36 amino acids in SSTI indicates homology with other members of the trypsin-inhibitor family from different sources. This inhibitor is highly stable in the presence of denaturing agents. SSTI showed significant inhibitory activity against trypsin-like proteases present in the larval midgut on Anagasta kuehniella, Corcyra cephalonica, Diatreae saccharalis and Anticarsia gemmatalis. |
Subject: | Trypsin inhibitor Sapindaceae Lepidopteran Kinetic studies |
Country: | EUA |
Editor: | Springer |
Rights: | fechado |
Identifier DOI: | 10.1007/s10930-010-9296-7 |
Date Issue: | 2011 |
Appears in Collections: | Unicamp - Artigos e Outros Documentos |
Files in This Item:
File | Description | Size | Format | |
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WOS000286464400002.pdf | 462.47 kB | Adobe PDF | View/Open |
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