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. 1984 Jul;159(1):410–412. doi: 10.1128/jb.159.1.410-412.1984

Porin isolated from the cell envelope of Rhodopseudomonas capsulata.

H T Flammann, J Weckesser
PMCID: PMC215650  PMID: 6330045

Abstract

The isolate major outer membrane protein from Rhodopseudomonas capsulata St. Louis (ATCC 23782) has a high porin activity in reconstituted phospholipid liposomes. The pore size of the homooligomeric porin with subunits of Mr 33,000 was determined to be about 0.8 nm in radius. Circular dichroism data revealed major portions of the beta structure. Heating of the oligomer resulted in monomer formation, loss of porin activity (60 to 70 degrees C), and change to alpha structure (100 degrees C).

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Selected References

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