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Leukotriene C4 form...
Leukotriene C4 formation catalyzed by three distinct forms of human cytosolic glutathione transferase.
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- Söderström, M (author)
- Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden
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- Mannervik, B (author)
- Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden
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- Orning, L (author)
- Department of Physiological Chemistry, Karolinska Institutet, S-104 01 Stockholm, Sweden
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- Hammarström, S (author)
- Department of Physiological Chemistry, Karolinska Institutet, S-104 01 Stockholm, Sweden
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(creator_code:org_t)
- 1985
- 1985
- English.
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In: Biochemical and Biophysical Research Communications - BBRC. - 0006-291X .- 1090-2104. ; 128:1, s. 265-70
- Related links:
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https://urn.kb.se/re...
Abstract
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- 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.
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