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Partial Characterization of Thymocyte‐Activating Factor Derived from MDP‐Stimulated Guinea Pig Fibroblasts
Author(s) -
Iribe Hideaki,
Koga Toshitaka
Publication year - 1984
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1984.tb00770.x
Subject(s) - thymocyte , sepharose , trypsin , protease , biology , phosphate , agarose , tris , potassium phosphate , guinea pig , microbiology and biotechnology , chromatography , chymotrypsin , biochemistry , chemistry , enzyme , t cell , immunology , immune system , endocrinology
The activity of fibroblast‐derived thymocyte activating factor (FTAF) of the guinea pig was measured, and the factor was partially characterized. The FTAF activity was heat labile, and destroyed by treatment with trypsin, chymotrypsin, and Streptomyces griseus protease, suggesting the protein nature of FTAF. FTAF bound to DEAE‐Sepharose CL‐6B in Tris‐HCl buffer at pH 8.0, and was eluted with 0.1–0.2 M NaCl. FTAF was absorbed with Blue Sepharose CL‐6B. The factor bound to a hydroxylapatite column in 10 mM phosphate buffer and was eluted in two major fractions, one fraction with 40 mM phosphate buffer, the other with 70–110 mM phosphate buffer. Finally, FTAF did not have as much effect on the proliferation of lymph node T cells as T‐cell‐activating monokines which exhibited marked stimulating effects on both T lymphocytes and thymocytes.