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Moeller, J. ; Hültner, L.* ; Schmitt, E.* ; Breuer, M.* ; Dörmér, P.G.*

Purification of MEA, a mast cell growth-enhancing activity, to apparent homogeneity and its partial amino acid sequencing.

J. Immunol. 144, 4231-4234 (1990)
DOI
Open Access Green as soon as Postprint is submitted to ZB.
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.
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Publication type Article: Journal article
Document type Scientific Article
ISSN (print) / ISBN 0022-1767
e-ISSN 1550-6606
Journal Journal of Immunology
Quellenangaben Volume: 144, Issue: 11, Pages: 4231-4234 Article Number: , Supplement: ,
Publisher American Association of Immunologists
Reviewing status Peer reviewed
Institute(s) Institut für Experimentelle Hämatologie
Institut für Immunologie