Isolation of principal outer membrane protein and antigen of Chl

Chemistry: analytical and immunological testing – Involving immune complex formed in liquid phase – Separation of immune complex from unbound antigen or antibody

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436543, 436544, 436545, 436546, 436547, 435 7, 260112R, 260112B, G01N 3356, G01N 3358, G01N 3360, C07G 700

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044277822

ABSTRACT:
Procedures are presented for isolating the major outer membrane protein of Chlamydia trachomatis. The isolated protein is a species specific antigen which comprises about 60% of the C. trachomatis cell outer membrane structure. The protein has a molecular weight ranging from about 38,000 to 44,000 daltons, with a mean molecular weight of about 39,500 daltons. The protein antigen is purified from C. trachomatis cells by first extracting the cell contents with a mild anionic detergent, preferably sarcosyl, to leave a residue of intact outer cell membranes. These outer cell membranes are then extracted with a strong anionic detergent, preferably sodium dodecyl sulfate, which solubilizes the 39,500 dalton antigen. The antigen is then purified by hydroxlapatite chromatography. The antigen is species specific for Chlamydia trachomatis and may be utilized in assaying Chlamydial infection in mammals.

REFERENCES:
patent: 4118469 (1978-10-01), Caldwell et al.
Taylor-Robinson et al., Lancet, 2 Jun. 1979, pp. 1162-1163.
Schuller et al., Lancet, 6 Jan. 1979, pp. 19-20.
Banks et al., Infection and Immunity, vol. 20, 1978, pp. 864-866.
Caldwell et al., Infection and Immunity, vol. 31, 1981, pp. 1161-1176.
Caldwell et al., J. Immunol., vol. 115, 1975, pp. 969-975.
Caldwell et al., J. Immunol., vol. 118, 1977, pp. 437-441.
Caldwell et al., J. Immunol., vol. 118, 1977, pp. 442-445.

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