Hirashima Y, Farooqui A A, Horrocks L A
Department of Physiological Chemistry, Ohio State University, Columbus 43210.
Biochem J. 1989 Jun 1;260(2):605-8. doi: 10.1042/bj2600605.
We developed a continuous spectrofluorimetric assay of lysoplasmalogenase activity with the use of horse liver alcohol dehydrogenase as a coupling enzyme. In this method the disappearance of NADH is measured spectrofluorimetrically. The excitation and emission monochromators were set at 340 and 460 nm respectively. The assay is 10 times as sensitive as the previous u.v. spectrophotometric method. We could detect approx. 0.02 nmol of aldehyde produced/min per ml.
我们利用马肝醇脱氢酶作为偶联酶,开发了一种连续荧光分光光度法来测定溶血缩醛磷脂酶活性。在该方法中,通过荧光分光光度法测定NADH的消失量。激发和发射单色仪分别设置在340和460nm。该测定方法的灵敏度是先前紫外分光光度法的10倍。我们能够检测到每毫升每分钟约产生0.02nmol的醛。