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

页码：519 / 523

页数：5

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