Detachment and chemical characterization of the regularly arranged subunits from the surface of an Acinetobacter.
Acinetobacter sp. strain MJT/F5/199A carries an array of tetragonally arranged subunits on its outer surface. The subunits can be detached from isolated cell walls by incubation with 1 M urea or by washing with water after treatment with 10 mM ethylenediaminetetraacetic acid or ethyleneglycol-bis(beta-aminoethylether)N,N'-tetraacetic acid. After removal of the urea, they reaggregate into the same ordered array at air-water interfaces in the presence of MgCl(2). The detached subunits were characterized as an acidic protein of molecular weight 65,000. They represent one-fifth of the total cell wall protein.
D000421:Alcaligenes / Q000032:analysis / Q000166:cytology*; D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000032:analysis* / Q000302:isolation & purification; D002458:Cell Fractionation; D002473:Cell Wall / Q000032:analysis*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004492:Edetic Acid; D004589:Electrophoresis, Disc; D006146:Guanidines; D008274:Magnesium; D008722:Methods; D008854:Microscopy, Electron; D008970:Molecular Weight; D014508:Urea
D000596:Amino Acids; D001426:Bacterial Proteins; D006146:Guanidines; D014508:Urea; D004492:Edetic Acid; D008274:Magnesium