Kikuta Y, Kusunose E, Kondo T, Yamamoto S, Kinoshita H, Kusunose M
Department of Food Science and Technology, Faculty of Engineering, Fukuyama University, Hiroshima, Japan.
FEBS Lett. 1994 Jul 4;348(1):70-4. doi: 10.1016/0014-5793(94)00587-7.
We have isolated and sequenced a cDNA for human liver LTB4 omega-hydroxylase. The cDNA encoded a protein of 520 amino acids with a molecular weight of 59,853 Da. The cDNA-deduced amino acid sequence showed 87.3% homology to that of human polymorphonuclear leukocytes (PMN) LTB4 omega-hydroxylase (CYP4F3). Northern blot analysis revealed that the mRNA hybridized to the specific cDNA fragment is expressed in human liver, but not in human PMN. The microsomes from yeast cells transfected with the cDNA catalyzed the omega-hydroxylation of LTB4 with a Km of 44.8 microM. These results clearly show that a new form of the CYP4F LTB4 omega-hydroxylase exists in human liver.
我们已经分离并测序了人肝脏白三烯B4ω-羟化酶的cDNA。该cDNA编码一个由520个氨基酸组成的蛋白质,分子量为59,853道尔顿。cDNA推导的氨基酸序列与人多形核白细胞(PMN)白三烯B4ω-羟化酶(CYP4F3)的序列具有87.3%的同源性。Northern印迹分析显示,与特定cDNA片段杂交的mRNA在人肝脏中表达,但在人PMN中不表达。用该cDNA转染的酵母细胞微粒体催化白三烯B4的ω-羟化反应,Km为44.8微摩尔。这些结果清楚地表明,人肝脏中存在一种新形式的CYP4F白三烯B4ω-羟化酶。