title: Partial purification and characterization of a colony-stimulating factor secreted by a T lymphocyte clone.
abstract: The mouse T lymphocyte clone L2 secretes a minimum of 10 lymphokine activities affecting at least 5 different target cells. Large amounts of colony-stimulating factor (CSF) (8.6 X 10(6) U/ml) can be obtained by stimulating L2 cells with concanavalin A. The major CSF activity secreted by L2 cells has been enriched to a specific activity of approximately 2-4 X 10(8) colonies/mg of protein using hydrophobic-interaction, gel-permeation, ion-exchange, and lectin-affinity chromatography. This preparation of CSF contains no detectable interleukin 2, interleukin 3, or interferon. The major L2-cell CSF induces granulocyte/macrophage colonies from bone marrow cells. This GM CSF has an apparent Mr of 22,000 as determined by gel-permeation chromatography. Treatment of L2-cell CSF with proteolytic enzymes abrogates biologic activity.
mesh_terms: D000818:Animals; D002460:Cell Line; D002845:Chromatography; D002851:Chromatography, High Pressure Liquid; D002999:Clone Cells / Q000378:metabolism; D003115:Colony-Stimulating Factors / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D003208:Concanavalin A / Q000494:pharmacology; D051379:Mice; D008808:Mice, Inbred CBA; D008811:Mice, Inbred DBA; D010447:Peptide Hydrolases / Q000494:pharmacology; D013601:T-Lymphocytes / Q000378:metabolism*
chemical_list: D003115:Colony-Stimulating Factors; D003208:Concanavalin A; D010447:Peptide Hydrolases