ArticleProceedings of the National Academy of Sciences of the United States of America1992
Purification of human leukotriene C4 synthase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 80 citations in OpenAlex.
- Article
- Cross-Talk between Cancer Cells and the Tumour Microenvironment: The Role of the 5-Lipoxygenase Pathway.International journal of molecular sciences · 2017Review
- The nuclear membrane leukotriene synthetic complex is a signal integrator and transducer.Molecular biology of the cell · 2012Article
- Oxidative stress suppresses cysteinyl leukotriene generation by mouse bone marrow-derived mast cells.The Journal of biological chemistry · 2011Article
- The membrane organization of leukotriene synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The organization and consequences of eicosanoid signaling.The Journal of clinical investigation · 2003Review
- Leukotriene D4 and cystinyl-bis-glycine metabolism in membrane-bound dipeptidase-deficient mice.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Eosinophil lipid bodies: specific, inducible intracellular sites for enhanced eicosanoid formation.The Journal of experimental medicine · 1997Article
- Leukotriene activity modulation in asthma.Drugs · 1997Review
- Hepatobiliary excretion of cysteinyl leukotrienes in three experimental models of acute hepatic injury.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 1996Article
- Expression cloning of a cDNA for human leukotriene C4 synthase, an integral membrane protein conjugating reduced glutathione to leukotriene A4.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- LTC4 synthase. Enzymology, biochemistry, and molecular characterization.Clinical reviews in allergy & immunologyReview
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Leukotriene (LT) C4 synthase, the enzyme that catalyzes the conjugation of LTA4 with reduced glutathione to form LTC4, was purified to homogeneity from the KG-1 myeloid cell line after solubilization of the microsomes utilizing a combination of 0.4% sodium deoxycholate and 0.4% Triton X-102. The solubilized enzyme was then applied to an S-hexyl-glutathione-agarose column that was eluted by the use of 7.5 mM probenecid. After removal of the probenecid by sequential concentration and dilution in an Amicon concentrator, the enzyme was additionally purified and concentrated by binding to and elution from approximately 75 mg of S-hexyl-glutathione-agarose. The enzyme was further resolved by electrophoresis with a nondenaturing Tris-glycine gel, and the LTC4 synthase activity was localized to slices 3 and 4. When the remainder of the eluate from the nondenaturing gel was precipitated by acetone and analyzed by 14% SDS/PAGE with silver staining, a single protein band of 18 kDa was associated with LTC4 synthase activity and was not present in the eluates of slices lacking activity. The overall recovery was 12.5%. In a separate preliminary purification, in which the yield was only approximately 1%, the eluates of the nondenaturing gel had also revealed a single protein of 18 kDa by SDS/PAGE, which was present only in the eluates with LTC4 synthase activity. These data identify LTC4 synthase as a protein of 18 kDa, a size consistent with its membership in the microsomal glutathione S-transferase family.
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