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Leukotriene C4 synthase: characterization in mouse mastocytoma cells
Stockholm University, Sweden.ORCID iD: 0000-0003-3927-4394
Uppsala University, Sweden.
Linköping University, Department of Biomedicine and Surgery, Cell biology. Linköping University, Faculty of Health Sciences.
1990 (English)In: Methods in Enzymology, ISSN 0076-6879, Vol. 187, 306-312 p.Article in journal (Refereed) Published
Abstract [en]

The chapter presents a study on leukotriene C4 (LTC4) synthase, discussing the characterization in mouse mastocytoma cells. LTC4 is formed by conjugation of leukotriene A4 (LTA4) with glutathione (GSH). In biological systems, the reaction is catalyzed by a membrane-bound enzyme, leukotriene C4 synthase (EC Cytosolic glutathione transferases, in particular, members of the class Mu, have been shown to catalyze formation of LTC4.The most efficient isoenzymes are transferase 6-6 isolated from rat brain, transferase 4-4 from rat liver, and transferase μ from human liver. The name leukotriene C4 synthase, used for the enzyme described in this chapter, has been adopted to distinguish the enzyme from the above glutathione transferases, which display broad substrate specificity. Reports from three groups of investigators have shown that LTC4 formation in rat basophilic leukemia cells is catalyzed by a membrane-bound enzyme. Leukotriene C4 synthase activity has been described and an enzyme partially purified from the microsomal fraction of guinea pig lung. The formation of LTC4 is especially high in mouse mastocytoma cells, the source from which LTC4 was first isolated. The partial purification of leukotriene C4 synthase from this source is described in the chapter.

Place, publisher, year, edition, pages
Elsevier, 1990. Vol. 187, 306-312 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-99874ISI: A1990EF62500032PubMedID: 2172733OAI: diva2:658713
Available from: 2013-10-22 Created: 2013-10-22 Last updated: 2013-10-31Bibliographically approved

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Söderström, MatsHammarström, Sven
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