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On the nature of leukotriene C4 synthase in human platelets
Wallenberg Laboratory, Stockholm University, Sweden.ORCID iD: 0000-0003-3927-4394
Uppsala University, Sweden.
Pennsylvania State University, USA.
Linköping University, Department of Biomedicine and Surgery, Cell biology. Linköping University, Faculty of Health Sciences.
1992 (English)In: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 294, no 1, 70-74 p.Article in journal (Refereed) Published
Abstract [en]

Leukotriene C4 is considered to play a major role in several important pathophysiological conditions, e.g., allergy, asthma, and shock. The present investigation demonstrates the presence in human platelets of a membrane-associated enzyme catalyzing the final step in the biosynthesis of leukotriene C4. This leukotriene C4 synthase was shown to be distinct from previously characterized "microsomal" and soluble glutathione transferases. The latter enzymes did not contribute significantly to the leukotriene A4 conjugating activity in platelets. As determined with leukotriene C4 synthase of a crude membrane fraction from human platelets, the Km value was 7 microM and the V value was 0.56 nmol x min-1 x mg-1 with leukotriene A4 as substrate. The enzyme was 20-fold more efficient with leukotriene A4 than with leukotriene A5 and 30-fold more efficient than with the unphysiological derivative leukotriene A4 methyl ester, as measured by the corresponding V/Km values; 14,15-leukotriene A4 was not a substrate. Platelets should be a useful source for the purification and further characterization of human leukotriene C4 synthase.

Place, publisher, year, edition, pages
Elsevier, 1992. Vol. 294, no 1, 70-74 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-99877ISI: A1992HJ44600011PubMedID: 1312812OAI: diva2:658720
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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