Isolation and Characterization of a New Trypsin Inhibitor from Crotalaria paulina Seeds

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 isoelectri...

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Veröffentlicht in:IUBMB life 1999-11, Vol.48 (5), p.519-523
Hauptverfasser: Pando, Luiza A., Ciero, Luciana Di, Novello, Jose C., Oliveira, Benedito, Weder, Jurgen K. P., Marangoni, Sergio
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Sprache:eng
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Zusammenfassung: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.
ISSN:1521-6543
1521-6551
DOI:10.1080/713803553