Shapiro R, Riordan J F, Vallee B L
Biochemistry. 1986 Jun 17;25(12):3527-32. doi: 10.1021/bi00360a008.
Angiogenin, a blood vessel inducing protein isolated from a human tumor cell line, has been found to exhibit ribonucleolytic activity. It catalyzes the cleavage of both 28S and 18S ribosomal RNA as determined by agarose gel electrophoresis. The major products formed with these substrates are 100-500 nucleotides in length. In contrast, angiogenin is inactive toward all of the more conventional substrates of the homologous pancreatic ribonucleases. In particular, it does not produce detectable amounts of acid-soluble fragments from high molecular weight wheat germ RNA, poly(C), or poly(U), nor does it hydrolyze cytidine or uridine cyclic 2',3'-phosphate. The high degree of sequence homology between angiogenin and the pancreatic ribonucleases, which includes all three catalytic residues, His-12, Lys-41, and His-119, has thus identified the chemical nature of a potential angiogenin substrate. These results may bear importantly on the physiological function of angiogenin.
血管生成素是一种从人肿瘤细胞系中分离出的血管诱导蛋白，已发现它具有核糖核酸酶活性。通过琼脂糖凝胶电泳测定，它能催化28S和18S核糖体RNA的切割。与这些底物形成的主要产物长度为100 - 500个核苷酸。相比之下，血管生成素对同源胰腺核糖核酸酶的所有更传统底物均无活性。具体而言，它不会从高分子量小麦胚芽RNA、聚（C）或聚（U）产生可检测量的酸溶性片段，也不会水解胞苷或尿苷环2',3'-磷酸。血管生成素与胰腺核糖核酸酶之间高度的序列同源性，包括所有三个催化残基，即His - 12、Lys - 41和His -
