Pore-forming ability of major outer membrane proteins from Wolinella recta ATCC 33238.
Three major outer membrane proteins with apparent molecular masses of 43, 45, and 51 kDa were purified from Wolinella recta ATCC 33238, and their pore-forming abilities were determined by the black lipid bilayer method. The non-heat-modifiable 45-kDa protein (Omp 45) showed no pore-forming activity even at high KCl concentrations. The single-channel conductances in 1 M KCl of the heat-modifiable proteins with apparent molecular masses of 43 kDa (Omp 43) and 51 kDa (Omp 51) were 0.49 and 0.60 nS, respectively. The proteins formed nonselective channels and, as determined by experiments of ion selectivity and zero-current potential, were weakly anion selective.
Department of Periodontics, University of Texas Health Science Center-San Antonio 78284-7894.
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Kennell
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Egli
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Hancock
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Holt
D001425:Bacterial Outer Membrane Proteins / Q000276:immunology / Q000302:isolation & purification*; D002712:Chlorides / Q000378:metabolism; D007473:Ion Channels / Q000502:physiology*; D008970:Molecular Weight; D018272:Porins; D011188:Potassium / Q000378:metabolism; D016968:Wolinella / Q000737:chemistry* / Q000502:physiology
D001425:Bacterial Outer Membrane Proteins; D002712:Chlorides; D007473:Ion Channels; D018272:Porins; D011188:Potassium