Summary: A protein with a molecular mass of 64 kDa (P64) from serovar was partially purified by using successively, phase partitioning with Triton X-114, ion-exchange chromatography and sucrose gradient centrifugation. Purification to homogeneity was obtained by electroelution of P64 from SDS-polyacrylamide gels. Monospecific rabbit antiserum (RαP64) was prepared using the purified protein preparation. P64 had a native molecular mass of > 670 kDa and was recognized by RαP64 as well as by human antisera. Western blotting of leptospiral serovars and 18 other bacterial species with RαP64 showed that P64 was cross-reactive with an equivalent antigen in a wide range of bacteria, indicating that it belongs to a family of antigens previously designated ‘common antigen’. This putative common antigen from appears to have a sub-surface location, but its function is not yet known.


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