| Literature DB >> 21127952 |
Maria Lígia R Macedo1, Eduardo B S Diz Filho, Mariadas Graças M Freire, Maria Luiza V Oliva, Joana T Sumikawa, Marcos H Toyama, Sérgio Marangoni.
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 NH₂- 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.Entities:
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Year: 2011 PMID： 21127952 DOI： 10.1007/s10930-010-9296-7
Source DB: PubMed Journal: Protein J ISSN： 1572-3887 Impact factor: 2.371