酵素を用いるプロスタグランディンの螢光定量について

概要

論文の詳細を見る
For the quantitative determination of prostaglandin, prostaglandins dehydrogenase dependent on nicotinamide adenine dinucleotide (NAD^+) was purified from swinelung. This enzyme catalyzed the oxidation of secondary alcohol group at C-15 in prostaglandin to a ketone, and the coenzyme NAD^+ was reduced to NADH. For higher sensitivity, this assav method was coupled with the reduction of resazurin, as catalyzed by diaphorase in the presence of a catalytic amount of NADH, and resorufin formed during this enzymic reaction was measured by a very sensitive fluorometry. This method made it possible to measure 4×10^<-11> mole of prostaglandin.
公益社団法人日本薬学会の論文
1972-09-25