Characterization of microsomal GST-II by western blot and identification of a novel LTC4 isomer.
Protein expression of microsomal GST-II and LTC4 synthase was analyzed by Western blot. Correlation between a 17 kDa band and LTC4 formation was observed for both enzymes. The expression of microsomal GST-II was several fold more efficient than the expression of LTC4 synthase. In addition to catalyzing the biosynthesis of LTC4, microsomal GST-II also produces another product, which has been subjected to mass spectrometric analysis. This analysis demonstrates that the novel product is an isomer of LTC4.
Jakobsson
P J
PJ
Merck Frosst Centre For Therapeutic Research, Kirkland, Quebec, Canada. Per-Johan.Jakobsson@mbb.ki.se
Scoggan
K A
KA
Yergey
J
J
Mancini
J A
JA
Ford-Hutchinson
A W
AW
D000818:Animals; D015153:Blotting, Western; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D005982:Glutathione Transferase / Q000737:chemistry* / Q000378:metabolism; D007536:Isomerism; D017997:Leukotriene C4 / Q000737:chemistry*; D013058:Mass Spectrometry; D008861:Microsomes / Q000201:enzymology*; D018411:Spodoptera
D017997:Leukotriene C4; D005982:Glutathione Transferase; C041116:leukotriene-C4 synthase