Gagnon C, Axelrod J, Musto N, Dym M, Bardin C W
Endocrinology. 1979 Dec;105(6):1440-5. doi: 10.1210/endo-105-6-1440.
Protein carboxyl-methylase (PCM), the enzyme that transfers methyl groups from S-adenosyl-methionine to free carboxyl groups on proteins, is highly localized in testes. The cellular distribution of PCM and its substrates, the methyl acceptor proteins, was investigated. Separation of testicular cells on an albumin gravity gradient revealed the preferential localization of both enzyme and substrates in spermatids. In young rats, PCM activity increases with age coincidently with germ cell maturation. Rats which are heterozygous for the Hre gene (Hre/+) are infertile as a result of germ cell depletion. In these animals, testicular PCM specific activity and total activity were, respectively, 4--6 and 40--50 times lower than in normal testes. Enzyme activity in testes from animals with x-ray-induced germ cell depletion was also very low. These observations suggest that PCM is located in germ cells.
蛋白质羧甲基酶(PCM)是一种将甲基从S-腺苷甲硫氨酸转移至蛋白质上游离羧基的酶,在睾丸中高度富集。对PCM及其底物(甲基受体蛋白)的细胞分布进行了研究。通过白蛋白密度梯度对睾丸细胞进行分离,结果显示该酶及其底物在精子细胞中存在优先定位。在幼鼠中,PCM活性随着年龄增长以及生殖细胞成熟而增加。Hre基因杂合子(Hre/+)大鼠由于生殖细胞耗竭而不育。在这些动物中,睾丸PCM的比活性和总活性分别比正常睾丸低4至6倍和40至50倍。经X射线诱导生殖细胞耗竭的动物睾丸中的酶活性也非常低。这些观察结果表明PCM位于生殖细胞中。