The affinity of a mycobacterial glycopeptide for guinea-pig gamma-globulin.

The affinity of a glycopeptide from culture filtrates of for guinea-pig serum components, first observed as an alteration of electrophoretic mobility of γ-immunoglobulin in agar has been explored by a variety of techniques. It was shown that such changes in mobility were produced more readily with γ-globulin (Fraction I from DEAE cellulose chromatography) than with γ-globulin (Fraction III from DEAE cellulose chromatography). It was estimated that the treatment resulted in a rise of carbohydrate associated with γ-globulin from 1.3 per cent to 38–40 per cent.