Purification of Aeromonas hydrophila major outer-membrane proteins: N-terminal sequence analysis and channel-forming properties.

Abstract:

: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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Jeanteur D,Gletsu N,Pattus F,Buckley JT

doi

10.1111/j.1365-2958.1992.tb02203.x

subject

Has Abstract

pub_date

1992-11-01 00:00:00

pages

3355-63

issue

22

eissn

0950-382X

issn

1365-2958

journal_volume

6

pub_type

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