Please use this identifier to cite or link to this item: 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

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