Abstract
Extraction of membranes of Mycoplasma hominis with n-butanol showed that antigenicity was associated with the non-lipid residue, which probably consisted mainly of protein, and not with the lipid itself.
Since many membrane proteins are hydrophobic, membranes were rendered soluble in various ways. Extraction with urea or phenol was the most successful, yielding extracts which were both antigenic and serologically reactive. The urea extract could not be fractionated by polyacrylamide disk electrophoresis or by column chromatography. However, serologically active components identified by gel diffusion were separated from detergent-lysed membranes by polyacrylamide disk electrophoresis. The activities of antisera against these fractions suggested that indirect-haemagglutinating or metabolic-inhibiting antibodies can be directed against several different membrane antigens. However, the antigens identified by gel diffusion probably do not represent all the components participating in indirect haemagglutination.
Treatment of membrane suspensions with heat, alkali, periodate and various enzymes showed that the four components identified by gel diffusion could be distinguished by their differing stabilities and properties. On the basis of their lability and susceptibility to proteolytic enzymes, two were identified as proteins.
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