The isolation by immunoabsorbent affinity chromatography and physicochemical characterization of Mycobacterium tuberculosis antigen 5.
Mycobacterium 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 was found to have a molecular weight 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.
D001426:Bacterial Proteins / Q000302:isolation & purification; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D007122:Immunoelectrophoresis; D007163:Immunosorbent Techniques; D009169:Mycobacterium tuberculosis / Q000276:immunology*; D014373:Tuberculin / Q000302:isolation & purification*
D001426:Bacterial Proteins; C016603:Mycobacterium tuberculosis antigen 5; D014373:Tuberculin