Formation of leukotriene B4-coenzyme A ester by rat liver microsomes.
When leukotriene B4 (LTB4) was incubated with rat liver microsomal fraction in the presence of coenzyme A (CoA) and ATP, a more polar product (compound I) was detected on reverse-phase high-performance liquid chromatography (RP-HPLC). The product was identified as LTB4-CoA ester on the basis of ultraviolet spectrometry, alkaline hydrolysis followed by RP-HPLC, and fast atom bombardment mass spectrometry (FAB-MS). The activity forming LTB4-CoA ester was localized in the microsomal fraction. The reaction was proportional to the concentration of the microsomal protein with an optimal pH of 7.5-8.0 and completely dependent on CoA and ATP. Palmitic acid and myristic acid significantly inhibited the formation.
Yamaoka
A
A
Department of Biochemistry, Kyushu University School of Medicine, Fukuoka, Japan.
Sumimoto
H
H
Isobe
R
R
Minakami
S
S
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003065:Coenzyme A / Q000378:metabolism*; D007975:Leukotriene B4 / Q000378:metabolism*; D008297:Male; D013058:Mass Spectrometry; D008862:Microsomes, Liver / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D007975:Leukotriene B4; D003065:Coenzyme A