ISOLATION AND CHARACTERIZATION OF ANGIOGENIN, AN ANGIOGENIC PROTEIN FROM HUMAN CARCINOMA-CELLS
ISOLATION AND CHARACTERIZATION OF ANGIOGENIN, AN ANGIOGENIC PROTEIN FROM HUMAN CARCINOMA-CELLS
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DOI：
10.1021/bi00341a030
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发表时间：
1985-01-01
期刊：
影响因子：
2.9
通讯作者：
VALLEE, BL
中科院分区：
文献类型：
--
作者：
FETT, JW;STRYDOM, DJ;VALLEE, BL
从已建立的人腺癌细胞系（HT-29）的无血清上清液中分离出首个具有体内血管生成活性的纯人类肿瘤来源蛋白，并命名为angiogenin。采用阳离子交换和反相高效液相色谱法纯化；收益率约为0.1%。0.5 .mu。g/L培养基。利用鸡胚绒毛尿囊膜法对纯化过程中血管生成素的生物活性进行监测。统计评估表明，它在该系统中显示的活性低至每蛋35 fmol。此外，只需要3.5 pmol就能诱导兔角膜血管的广泛生长。氨基酸组成的基本（等电点> 9.5），单链蛋白质的分子量。14,400已被确定。氨基端被阻断，羧基端残基是脯氨酸。
The first human tumor derived protein with in vivo angiogenic activity to be obtained in pure form has been isolated from serum-free supernatants of an established human adenocarcinoma cell line (HT-29) and named angiogenin. It was purified by cation-exchange and reversed-phase high-performance liquid chromatography; the yield was .apprx. 0.5 .mu.g/L of medium. Biological activity of angiogenin was monitored throughout purification by using the chick embryo chorioallantoic membrane assay. Statistical evaluation demonstrates that it displays activity in this system with as little as 35 fmol per egg. Moreover, only 3.5 pmol is required to induce extensive blood vessel growth in the rabbit cornea. The amino acid composition of this basic (isoelectric point > 9.5), single-chain protein of molecular weight .apprx. 14,400 has been determined. The amino terminus is blocked, and the carboxyl-terminal residue is proline.