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Leukotriene C4 formation catalyzed by three distinct forms of human cytosolic glutathione transferase.
Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden.ORCID iD: 0000-0003-3927-4394
Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden.
Department of Physiological Chemistry, Karolinska Institutet, S-104 01 Stockholm, Sweden.
Department of Physiological Chemistry, Karolinska Institutet, S-104 01 Stockholm, Sweden.
1985 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 128, no 1, 265-70 p.Article in journal (Refereed) Published
Abstract [en]

The ability of three distinct types of human cytosolic glutathione transferase to catalyze the formation of leukotriene C4 from glutathione and leukotriene A4 has been demonstrated. The near-neutral transferase (mu) was the most efficient enzyme with Vmax= 180 nmol X min-1 X mg-1 and Km= 160 microM. The Vmax and Km values for the basic (alpha-epsilon) and the acidic (pi) transferases were 66 and 24 nmol X min-1 X mg-1 and 130 and 190 microM, respectively. The synthetic methyl ester derivative of leukotriene A4 was somewhat more active as a substrate for all the three forms of the enzyme.

Place, publisher, year, edition, pages
1985. Vol. 128, no 1, 265-70 p.
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Medical and Health Sciences
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URN: urn:nbn:se:liu:diva-99871ISI: A1985AFC9600039PubMedID: 2985074OAI: oai:DiVA.org:liu-99871DiVA: diva2:658702
Available from: 2013-10-22 Created: 2013-10-22 Last updated: 2017-12-06

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Söderström, MHammarström, S

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