Purification of MEA, a mast cell growth-enhancing activity, to apparent homogeneity and its partial amino acid sequencing.
A novel growth factor for bone marrow derived murine mucosal type mast cells has been isolated from the conditioned medium of the Mlsa-reactive mouse Th cell line MLS-4.2. In proliferation assays this growth factor synergizes, like IL-4, with IL-3 on established mast cell lines and was therefore termed MEA: mast cell growth enhancing activity. MEA was characterized as a glycoprotein with a Mr range between 37,000 and 43,000. Apparent homogeneity was obtained by using a four-step purification scheme including cation exchange chromatography, Procion red affinity chromatography, IEF, and gel filtration. Inasmuch as MEA was N-terminally blocked during automated Edman-degradation, peptide fragments after digestion with trypsin were used for partial amino acid sequence determination. All evaluable MEA peptide fragments showed complete sequence homology to a recently purified and cloned novel T cell growth factor (P40/TCGF III), the mouse homologue of human IL-9.
Moeller
J
J
Institut für Experimentelle Hämatologie, Gesellschaft für Strahlen und Umweltforschung, Munich, FRG.
Hültner
L
L
Schmitt
E
E
Breuer
M
M
Dörmer
P
P
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006023:Glycoproteins / Q000302:isolation & purification; D006133:Growth Substances / Q000302:isolation & purification*; D007526:Isoelectric Point; D008407:Mast Cells / Q000166:cytology*; D051379:Mice; D008811:Mice, Inbred DBA; D008969:Molecular Sequence Data; D008970:Molecular Weight; D006377:T-Lymphocytes, Helper-Inducer / Q000032:analysis
D006023:Glycoproteins; D006133:Growth Substances