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 Microbioljournal_title
Molecular microbiologyauthors
Jeanteur D,Gletsu N,Pattus F,Buckley JTdoi
10.1111/j.1365-2958.1992.tb02203.xsubject
Has Abstractpub_date
1992-11-01 00:00:00pages
3355-63issue
22eissn
0950-382Xissn
1365-2958journal_volume
6pub_type
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