title: Isolation of the adherence protein of Mycoplasma pneumoniae by fractionated solubilization and size exclusion chromatography.
abstract: The 168-kDa adherence protein of M. pneumoniae was solubilized and purified to homogeneity. Optimal yield was obtained by pretreatment of whole M. pneumoniae cells with buffer containing 1% Chaps and subsequent extraction with octylglucosid at a detergent to protein ratio of 5 and at octylglycoside concentrations between 1.5 and 2%. Contaminating membrane proteins with high molecular masses were removed by pretreatment with 1% Chaps and proteins of low molecular masses by size exclusion chromatography.
authors.affiliation: Institut für Medizinische Mikrobiologie und Hygiene, Universität Freiburg.
authors.forename: E
authors.initials: E
authors.lastname: Jacobs
authors.forename: K
authors.initials: K
authors.lastname: Fuchte
authors.forename: W
authors.initials: W
authors.lastname: Bredt
mesh_terms: D018829:Adhesins, Bacterial; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002850:Chromatography, Gel / Q000379:methods; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D005960:Glucosides; D008970:Molecular Weight; D009177:Mycoplasma pneumoniae / Q000502:physiology*
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D003902:Detergents; D005960:Glucosides; C035471:adhesin, Mycoplasma pneumoniae; C018619:octyl-beta-D-glucoside