Lin J J, Daniels-McQueen S, Patino M M, Gaffield L, Walden W E, Thach R E
Department of Biology, Washington University, St. Louis, MO 63130.
Science. 1990 Jan 5;247(4938):74-7. doi: 10.1126/science.2294594.
Incubation of a 90-kilodalton ferritin repressor protein (FRP), either free or complexed with an L-ferritin transcript, with hemin or Co3+-protoporphyrin IX prevented subsequent repression of ferritin synthesis in a wheat germ extract. Neither FeCl3 in combinations with H2O2, nor Fe3+ or Fe2+ chelated with EDTA, nor Zn2+-protoporphyrin IX, nor protoporphyrin IX caused significant inactivation of FRP. FRP that had been inactivated by hemin remained chemically intact, as revealed by SDS-polyacrylamide gel electrophoresis. Inclusion of chelators of iron or free radical scavengers did not alter the inactivation produced by hemin. These and other results indicate that hemin derepresses ferritin synthesis in vitro.
将90千道尔顿的铁蛋白阻遏蛋白（FRP），无论是游离的还是与L-铁蛋白转录本复合的，与血红素或三价钴原卟啉IX一起温育，可防止随后在小麦胚芽提取物中铁蛋白合成的抑制。三氯化铁与过氧化氢的组合、与乙二胺四乙酸螯合的三价铁或二价铁、锌原卟啉IX或原卟啉IX均未导致FRP的显著失活。经SDS-聚丙烯酰胺凝胶电泳显示，被血红素失活的FRP在化学性质上保持完整。加入铁螯合剂或自由基清除剂不会改变血红素产生的失活作用。这些及其他结果表明，血红素在体外可解除铁蛋白合成的抑制。
