Yamaoka A, Sumimoto H, Isobe R, Minakami S
Department of Biochemistry, Kyushu University School of Medicine, Fukuoka, Japan.
Biochem Biophys Res Commun. 1988 Aug 15;154(3):1248-52. doi: 10.1016/0006-291x(88)90273-2.
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.
