Isolation and characterization of a new trypsin inhibitor from Crotalaria paulina seeds

被引：16
|
作者：
Pando, LA
Di Ciero, L
Novello, JC
Oliveira, B
Weder, JKP
Marangoni, S [1 ]
机构：
[1] Univ Estadual Campinas, Inst Biol, Dept Bioquim, BR-13083970 Campinas, SP, Brazil
[2] Univ Sao Paulo, ESALQ, Dept Fitopatol, Piracicaba, SP, Brazil
[3] Tech Univ Munich, Inst Lebensmittelchem, D-85748 Garching, Germany
来源：
IUBMB LIFE | 1999年 / 48卷 / 05期
关键词：
Crotalaria paulina; trypsin inhibitor;
D O I：
10.1080/152165499306621
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：519 / 523
页数：5
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