Rothenberg S P, Kyner D, Solomon G
Department of Medicine, Department of Veterans Affairs Medical Center, Brooklyn, NY.
Mt Sinai J Med. 1992 Mar;59(2):150-3.
A protein with a molecular weight of 27,500 was co-purified with the enzyme dihydrofolate reductase (molecular weight 22,000) from the liver of mice less than 8 weeks of age using a methotrexate-Sepharose affinity matrix. This 27.5 kDa protein crossreacts with dihydrofolate reductase against an antiserum raised to the purified 22 kDa enzyme. The protein could also reduce dihydrofolate to tetrahydrofolate, thus demonstrating the catalytic properties of dihydrofolate reductase. The expression of this 27.5 kDa protein also appears to be age-dependent because it could not be isolated from liver of mice older than four months.
使用甲氨蝶呤-琼脂糖亲和基质,从小于8周龄小鼠的肝脏中,与二氢叶酸还原酶(分子量22,000)共同纯化出一种分子量为27,500的蛋白质。这种27.5 kDa的蛋白质与二氢叶酸还原酶发生交叉反应,该反应针对的是用纯化的22 kDa酶制备的抗血清。该蛋白质还能将二氢叶酸还原为四氢叶酸,从而证明了二氢叶酸还原酶的催化特性。这种27.5 kDa蛋白质的表达似乎也与年龄有关,因为从四个月以上小鼠的肝脏中无法分离出该蛋白。