Detection of antibodies specific to sodium dodecyl sulfate-treated proteins

Heavy meromyosin (HMM) denatured by sodium dodecyl sulfate (SDS) was injected into guinea pigs, either in the presence of 1 mg SDS/mg protein or after chromatography on Sephadex G-10 to remove detergent excess. Antigen-antibody interactions were analyzed by the microcomplement fixation technique. When HMM was injected in the presence of excess of SDS, the microcomplement fixation curves exhibited two maxima; one was specific to the random coil configuration of heavy meromyosin or myosin, and the other was common to several SDS-protein complexes. The latter peak disappeared when the excess SDS was removed from the immunogen by chromatography. Results showed the presence of antibodies directed either against SDS or against the non-specific SDS protein link.