Abstract
The affinity of a glycopeptide from culture filtrates of Mycobacterium tuberculosis for guinea-pig serum components, first observed as an alteration of electrophoretic mobility of γ2-immunoglobulin in agar has been explored by a variety of techniques. It was shown that such changes in mobility were produced more readily with γ2-globulin (Fraction I from DEAE cellulose chromatography) than with γ1-globulin (Fraction III from DEAE cellulose chromatography). It was estimated that the treatment resulted in a rise of carbohydrate associated with γ2-globulin from 1.3 per cent to 38–40 per cent.
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