Isolation and characterization of a new trypsin inhibitor from Crotalaria paulina seeds
| Autor: | José C. Novello, Luiza A. Pando, Jürgen K. P. Weder, Sergio Marangoni, Benedito Oliveira, Luciana Di Ciero |
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| Rok vydání: | 2000 |
| Předmět: |
Swine
Trypsin inhibitor Clinical Biochemistry Biochemistry Serine medicine Genetics Animals Chymotrypsin Humans Trypsin Horses Molecular Biology Chromatography Plants Medicinal biology Kunitz STI protease inhibitor Plant Extracts Fabaceae Cell Biology Kinetics Isoelectric point Glycine Seeds biology.protein Cattle Leucine Isoelectric Focusing Trypsin Inhibitors medicine.drug |
| Zdroj: | IUBMB life. 48(5) |
| ISSN: | 1521-6543 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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