Winters D K, Clejan L A, Cederbaum A I
Department of Biochemistry, Mount Sinai School of Medicine, (CUNY), N.Y. 10029.
Biochem Biophys Res Commun. 1988 Jun 16;153(2):612-7. doi: 10.1016/s0006-291x(88)81139-2.
Rat liver microsomes catalyzed the oxidation of glycerol to a Nash-reactive material in a time- and protein-dependent manner. Omission of the glycerol or the microsomes or any of the components of the NADPH-generating system resulted in almost a complete loss of product formation. Apparent Km and Vmax values for glycerol oxidation were about 18 mM and 2.5 nmol formaldehyde per min per mg microsomal protein. Carbon monoxide inhibited glycerol oxidation indicating a requirement for cytochrome P-450. That the Nash-reactive material was formaldehyde was validated by a glutathione-dependent formaldehyde dehydrogenase positive reaction. These studies indicate that glycerol is not inert when utilized with microsomes or reconstituted mixed function oxidase systems, and that the production of formaldehyde from glycerol may interfere with assays of other substrates which generate formaldehyde as product.
大鼠肝脏微粒体以时间和蛋白质依赖性方式催化甘油氧化为对纳什试剂呈反应性的物质。省略甘油、微粒体或NADPH生成系统的任何组分几乎会导致产物形成完全丧失。甘油氧化的表观Km和Vmax值分别约为18 mM和每分钟每毫克微粒体蛋白2.5 nmol甲醛。一氧化碳抑制甘油氧化，表明需要细胞色素P - 450。通过谷胱甘肽依赖性甲醛脱氢酶阳性反应证实了对纳什试剂呈反应性的物质是甲醛。这些研究表明，当甘油与微粒体或重组混合功能氧化酶系统一起使用时并非惰性，并且甘油产生甲醛可能会干扰其他以甲醛为产物的底物的测定。
