ISOLATION BY IMMUNOABSORBENT AFFINITY CHROMATOGRAPHY AND PHYSICOCHEMICAL CHARACTERIZATION OF MYCOBACTERIUM-TUBERCULOSIS ANTIGEN-5

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Abstract
M. tuberculosis antigen 5 was purified from unheated culture filtrates by absorption onto an immunoabsorbent prepared with globulin from a monospecific goat antiserum and elution with 4.0 M urea at pH 9.0. The product was a homogeneous protein giving a single stainable band in acrylamide gel electrophoresis and a single precipitin arc in immunoelectrophoresis. It had a MW of 28,500 to 35,000 daltons and a sedimentation constant of 2.0. Amino acid analysis demonstrated it to be rich in aspartic acid, suggesting a cytoplasmic origin.