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 |
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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. |
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ISSN: | 1521-6543 1521-6551 |
DOI: | 10.1080/713803553 |