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- W2181567295 abstract "We havepurified amajor outer membrane protein fromAeromonas salmonicida. This42-kilodalton protein shared several physical characteristics with enterobacterial porins inthat itwasnoncovalently associated withthepeptidoglycan,itwasreleased fromthepeptidoglycan inthepresence of0.1M NaCland sodiumdodecyl sulfate, anditsmobility onsodium dodecyl sulfate-polyacrylamide gels wasdependent onthesolubilization temperature before electrophoresis. Whenaddedtotheaqueous solution bathing aplanar bilayer membrane it caused theconductance ofthemembrane toincrease byseveral orders of magnitude. Atlowerprotein concentrations, single channels withanaverage conductance of1.6nSin1M KCIwereincorporated into themembrane ina stepwise fashion. Evidence that theprotein formed alarge, relatively nonselective, water-filled channel wasobtained byperforming single-channel experiments atdifferent NaClconcentrations andinavariety ofdifferent salts. Current through thechannel wasalinear function oftheapplied voltage, andnoevidence of voltage gating wasobserved. Inaddition, weobtained evidence fora43-kilodalton channel-forming protein intheoutermembrane ofA.hydrophila withasimilar single-channel conductance asthe42-kilodalton protein in1M NaCl. Theouter cell envelope ofgram-negative bacteria contains three layers, aninner membrane, apeptidoglycan layer, andanoutermembrane (20). Theouter membrane hasbeenshowntobe abarrier forthepenetration ofawidevariety of compounds (18) while atthesametimepermitting thesize-dependent passage ofsmall molecules (8,16). Thismolecular-sievin g action of" @default.
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- W2181567295 date "1983-01-01" @default.
- W2181567295 modified "2023-10-03" @default.
- W2181567295 title "Purification andReconstitution inLipid Bilayer Membranes of anOuterMembrane, Pore-Forming Protein ofAeromonas salmonicida" @default.
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