6-methyltetrahydropterin and batyl-alcohol

The kinetics of inhibition of glyceryl-ether monooxygenase with 6-methyl-5,6,7,8-tetrahydropterin as cofactor (saturating) by the detergent Mega-10 with batyl alcohol and (RS)-3-(1-hexadecyloxy)-2-hydroxypropane-1-phosphocholine as substrates exhibited noncompetitive inhibition with apparent Ki values of 1.74 +/- 0.37 mM and 185 +/- 23 microM, respectively. Inhibition by octadecan-1-ol (with batyl alcohol as substrate in the presence of 2.3 mM Mega-10) was competitive with an apparent Ki value of 765 +/- 80 microM. The critical micelle concentration values of various solutions of Mega-10 were determined and used to show that the active ether-lipid substrates were in micelle form (for a water soluble substrate) or mixed micelle form (for substrates solubilised with Mega-10).

Topics: Animals; Buffers; Detergents; Fatty Acids; Fatty Alcohols; Glucosamine; Glyceryl Ethers; Kinetics; Micelles; Microscopy, Electron; Microsomes, Liver; Mixed Function Oxygenases; Pterins; Rats; Solubility; Substrate Specificity

Topics: Fatty Acids; Glucosamine; Glyceryl Ethers; Indicators and Reagents; Kinetics; Mixed Function Oxygenases; Platelet Activating Factor; Pterins