THE PURIFICATION OF A GROEL-LIKE STRESS PROTEIN FROM AEROBICALLY ADAPTED CAMPYLOBACTER-JEJUNI

被引:18
作者
TAKATA, T
WAI, SN
TAKADE, A
SAWAE, Y
ONO, J
AMAKO, K
机构
[1] KYUSHU UNIV,FAC MED,DEPT BACTERIOL,FUKUOKA 812,JAPAN
[2] KYUSHU UNIV,SCH HLTH SCI,FUKUOKA 812,JAPAN
关键词
CAMPYLOBACTER JEJUNI; STRESS PROTEIN; GROEL;
D O I
10.1111/j.1348-0421.1995.tb03245.x
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
From plate cultures of Campylobacter jejuni grown in room air a particulate protein of 62 kDa was isolated by ion-exchange chromatography. The protein had a square shape from the side view but when viewed from the top it had a star-shaped structure. The molecular size of the whole particle determined by gel filtration was 850 kDa which suggested the presence of 14 subunits of 62 kDa in each particle. The N-terminal 37 amino residues showed more than 80% homology with the sequence of these heat shock protein (HSP) 60 homologs of Chlamydia trachomatis, Helicobacter pylori, and Escherichia coli (GroEL). This protein is immunologically cross-reactive with the antiserum for the 60-kDa HSP of Yersinia enterocolitica. Production of the 62-kDa protein increased under heat stress and growth in an aerobic atmospheric environment. From these observations we concluded that the 62-kDa protein is a Campylobacter stress protein (Cj62) which belongs to the HSP 60 family.
引用
收藏
页码:639 / 645
页数:7
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