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.