PURIFICATION AND CHARACTERIZATION OF A FUNGAL PROTEASE SPECIFIC PROTEIN INHIBITOR (FPI-F) IN THE SILKWORM HEMOLYMPH

被引：49

作者：

EGUCHI, M

ITOH, M

CHOU, LY

NISHINO, K

机构：

[1] Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Kyoto 606, Japan

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1993年 / 104卷 / 03期

关键词：

D O I：

10.1016/0305-0491(93)90279-E

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：

1. One of fungal protease inhibitors (FPI-F) in the haemolymph of the silkworm, Bombyx mori, was purified by ammonium sulphate precipitation, acid and heat treatments, cation exchange chromatography on a CM-Toyopearl and hydrophobic chromatography on a butyl-Toyopearl column. About 2000-fold purification was achieved and 13% of the activity was recovered. 2. The inhibitor had a mol. wt of approx. 6000. The kinetic analysis showed that FPI-F inhibits fungal protease uncompetitively (K(i) = 8.6 x 10(-8) M) and formed equimolar complex with fungal protease. 3. FPI-F suppressed strongly fungal proteases and subtilisin but the inhibition of alpha-chymotrypsin and trypsin was extremely weak.

引用

页码：537 / 543

页数：7

共 33 条

[1]

ARAKAWA H, 1989, J BIOL CHEM, V264, P2350

[2] THE CYSTATINS - A NEW CLASS OF PEPTIDASE INHIBITORS [J].