PURIFICATION OF AEROMONAS-HYDROPHILA MAJOR OUTER-MEMBRANE PROTEINS - N-TERMINAL SEQUENCE-ANALYSIS AND CHANNEL-FORMING PROPERTIES

被引:28
作者
JEANTEUR, D
GLETSU, N
PATTUS, F
BUCKLEY, JT
机构
[1] EUROPEAN MOLEC BIOL LAB,W-6900 HEIDELBERG,GERMANY
[2] UNIV VICTORIA,DEPT BIOCHEM & MICROBIOL,VICTORIA V8W 3P6,BC,CANADA
关键词
D O I
10.1111/j.1365-2958.1992.tb02203.x
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
Four outer-membrane proteins of Aeromonas hydrophila were purified and their N-terminal sequences and channel-forming properties were determined. Three could be matched with proteins from other species. One was a maltoporin, as its level increased when cells were grown in maltose-containing media, and the channel it formed was blocked by maltose. Another was like OmpF and OmpC of Escherichia coli, except that its channel fluctuated much more rapidly. The third protein, which was produced in low-phosphate medium, exhibited several properties of the general anion porin PhoE. The fourth showed no similarity to any known proteins. It had a unique N-terminus and it formed small sharply-defined cation-selective channels. Two other proteins which corresponded to OmpW of Vibrio cholerae and E. coli OmpA were partly characterized.
引用
收藏
页码:3355 / 3363
页数:9
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