Isolation and characterization of a new trypsin inhibitor from Crotalaria paulina seeds |
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| Authors: | Pando L A Di Ciero L Novello J C Oliveira B Weder J K Marangoni S |
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| Institution: | Departamento de Bioquímica, Instituto de Biologia, Campinas, SP, Brasil. |
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| 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 Ki 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. |
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