Okada N, Shindo-Okada N, Sato S, Itoh Y H, Oda K, Nishimura S
Proc Natl Acad Sci U S A. 1978 Sep;75(9):4247-51. doi: 10.1073/pnas.75.9.4247.
The guanine insertion enzyme from Escherichia coli catalyzes exchange of guanine located at the first position of the anticodon of tRNA with radioactive guanine (N. Okada and S. Nishimura, unpublished data). tRNA isolated from various tumors, including slowly growing Morris hepatoma 7794A, incorporated considerable guanine with E. coli guanine insertion enzyme, whereas tRNA isolated from all normal tissues so far tested, except regenerating rat liver, incorporated scarcely any. In the rat ascites hepatoma AH7974, the guanine was mostly incorporated into minor isoaccepting species of tRNAAsp that contained the guanine residue instead of Q base in the first position of the anticodon. This is a sensitive and easy method for identifying unique tRNA species in tumor tissues.
来自大肠杆菌的鸟嘌呤插入酶催化位于tRNA反密码子第一位的鸟嘌呤与放射性鸟嘌呤的交换(N. 冈田和西村修,未发表数据)。从包括生长缓慢的莫里斯肝癌7794A在内的各种肿瘤中分离出的tRNA,与大肠杆菌鸟嘌呤插入酶结合了相当数量的鸟嘌呤,而到目前为止测试的所有正常组织(除再生大鼠肝脏外)分离出的tRNA几乎没有结合。在大鼠腹水肝癌AH7974中,鸟嘌呤大多掺入到tRNAAsp的次要同功受体种类中,这些种类在反密码子的第一位含有鸟嘌呤残基而非Q碱基。这是一种鉴定肿瘤组织中独特tRNA种类的灵敏且简便的方法。