一种分枝杆菌糖肽对豚鼠γ球蛋白的亲和力。

Stewart-Tull D E, Wilkinson P C, White R G

Immunology. 1965 Aug;9(2):151-60.

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.

一种来自[未提及具体来源]培养滤液的糖肽对豚鼠血清成分的亲和力，最初表现为琼脂中γ-免疫球蛋白电泳迁移率的改变，现已通过多种技术进行了探究。结果表明，γ-球蛋白（DEAE纤维素层析的I组分）比γ-球蛋白（DEAE纤维素层析的III组分）更容易产生这种迁移率变化。据估计，该处理使与γ-球蛋白相关的碳水化合物含量从1.3%升至38 - 40%。