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|Type:||Artigo de periódico|
|Title:||Isolation and characterization of a new trypsin inhibitor from Crotalaria paulina seeds|
Di Ciero, L
|Abstract:||A new trypsin inhibitor (CPTI) has been isolated from Crotalaria paulina seeds. Purification of the inhibitor was carried out by gel filtration, ion-exchange chromatography, and subsequent reversed-phase HPLC. The presence of a single polypeptide chain, with a molecular mass of 20 kDa and isoelectric point 4.0, was detected. The trypsin inhibitor had a K-i value of 4.5 x 10(-8) M and was capable of acting on human, bovine, and porcine trypsin and weakly on bovine chymotrypsin, Amino acid analysis showed that CPTI has a high content of aspartate, glutamate, leucine, serine, and glycine, having 177 amino acid residues in its composition. These data suggest that the protein belongs to the Kunitz-type trypsin inhibitors.|
|Editor:||Taylor & Francis Inc|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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