The isolation by immunoabsorbent affinity chromatography and physicochemical characterization of Mycobacterium tuberculosis antigen 5

Am Rev Respir Dis. 1978 Mar;117(3):533-9. doi: 10.1164/arrd.1978.117.3.533.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / isolation & purification
  • Chromatography, Affinity
  • Electrophoresis, Polyacrylamide Gel
  • Immunoelectrophoresis
  • Immunosorbent Techniques
  • Mycobacterium tuberculosis / immunology*
  • Tuberculin / isolation & purification*

Substances

  • Bacterial Proteins
  • Mycobacterium tuberculosis antigen 5
  • Tuberculin