Isolation of the adherence protein of Mycoplasma pneumoniae by fractionated solubilization and size exclusion chromatography.
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.
Jacobs
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Institut für Medizinische Mikrobiologie und Hygiene, Universität Freiburg.
Fuchte
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Bredt
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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*
D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D003902:Detergents; D005960:Glucosides; C035471:adhesin, Mycoplasma pneumoniae; C018619:octyl-beta-D-glucoside