Isolation and partial properties of a porin-like protein from Vibrio parahaemolyticus cell envelope.
The cell envelope of Vibrio parahaemolyticus pilot strain K-11 contains a major protein with an apparent molecular weight of 35,000 which was not solubilized with 2% sodium dodecyl sulfate (SDS) at 50 C for 30 min and was resistant to trypsin. The protein was extracted from the SDS-insoluble envelope with SDS containing 0.4 M NaCl and purified by acetone precipitation and gel filtration. The purified protein was completely dissociated into a monomer with a molecular weight of 35,000 in SDS at 60 C. The amino acid composition of the protein was nearly the same as that of porins from Escherichia coli and Salmonella typhimurium. Thus the protein seems to be porin-like.
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000302:isolation & purification*; D008970:Molecular Weight; D018272:Porins; D012967:Sodium Dodecyl Sulfate; D014357:Trypsin; D014736:Vibrio parahaemolyticus / Q000032:analysis*
D000596:Amino Acids; D001426:Bacterial Proteins; D008565:Membrane Proteins; D018272:Porins; D012967:Sodium Dodecyl Sulfate; D014357:Trypsin