AMINO-ACID SEQUENCE OF HUMAN-TUMOR DERIVED ANGIOGENIN
AMINO-ACID SEQUENCE OF HUMAN-TUMOR DERIVED ANGIOGENIN
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DOI：
10.1021/bi00341a031
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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：
STRYDOM, DJ;FETT, JW;VALLEE, BL
人类肿瘤血管生成素是第一个从人类来源中分离出来的纯形式的肿瘤血管生成因子，它的氨基酸序列和二硫键配对已经通过传统的测序技术进行了测定，并应用于纳米分子和亚纳米分子水平的材料。血管生成素是一种单链蛋白质，由123个氨基酸组成，序列如下：-lt；Glu1-Asp-Asn-Ser-Arg-Tyr-Thr-His-Phe-Leu-Thr-Gln-His-Tyr-Asp15-Ala-Lys-Pro-Gln-Gly-Arg-Asp-Asp-Arg-Tyr-Cys-Glu-Ser-Ile-Met30-Arg-Arg-Arg-Gly-Leu-Thr-Ser-Pro-Cys-Lys-Asp-Ile-Asn-Thr-Phe45-Ile-His-Gly-Asn-Lys-Arg-Ser-Ile-Lys-Ala-Ile-Cys-Glu-Asn-Lys60-Asn-Gly-Asn-Pro-His-Arg-Glu-Asn-Leu-Arg-Ile-Ser-Lys-Ser-Ser75-Phe-Gln-Val-Thr-Thr-Cys-Lys-Leu-His-Gly-Gly-Ser-Pro-Trp-Pro90-Pro-Cys-Gln-Tyr-Arg-Ala-Thr-Ala-Gly-Phe-Arg-Asn-Val-Val-Val105-Ala-Cys-Glu-Asn-Gly-Leu-Pro-Val-His-Leu-Asp-Gln-SerIle-Phe120-Arg-Arg-Pro123-OH.三个二硫键连接半胱氨基残基26-81、39-92和57-107。该序列与胰腺核糖核酸酶的序列有35%的同源性，许多剩余的残基被保守地替换。核糖核酸酶的主要活性部位残基His-12、Lys-41和His-119与四个二硫键中的三个一样保守，相似性尤其明显。一种独特的人类器官起源信使分子的完整化学特征，即可以诱导器官形成的分子，实现了对器官发生特别是血管形成的长期研究的第一个主要目标。与核糖核酸酶意想不到的同源性为研究血管生成的生物过程提供了新的方法。
The amino acid sequence and disulfide bond pairing of human tumor derived angiogenin, the first tumor angiogenesis factor to be isolated in pure form from human sources, have been determined by conventional sequencing techniques adapted and applied to nanomole and subnanomole levels of material. Angiogenin, obtained from conditioned media of a human colonic adenocarcinoma cell line, is a single-chain protein consisting of 123 amino acids with the following sequence: < Glu1-Asp-Asn-Ser-Arg-Tyr-Thr-His-Phe-Leu-Thr-Gln-His-Tyr-Asp15-Ala-Lys-Pro-Gln-Gly-Arg-Asp-Asp-Arg-Tyr-Cys-Glu-Ser-Ile-Met30-Arg-Arg-Arg-Gly-Leu-Thr-Ser-Pro-Cys-Lys-Asp-Ile-Asn-Thr-Phe45-Ile-His-Gly-Asn-Lys-Arg-Ser-Ile-Lys-Ala-Ile-Cys-Glu-Asn-Lys60-Asn-Gly-Asn-Pro-His-Arg-Glu-Asn-Leu-Arg-Ile-Ser-Lys-Ser-Ser75-Phe-Gln-Val-Thr-Thr-Cys-Lys-Leu-His-Gly-Gly-Ser-Pro-Trp-Pro90-Pro-Cys-Gln-Tyr-Arg-Ala-Thr-Ala-Gly-Phe-Arg-Asn-Val-Val-Val105-Ala-Cys-Glu-Asn-Gly-Leu-Pro-Val-His-Leu -Asp-Gln-Ser-Ile-Phe120-Arg-Arg-Pro123-OH. Three disulfide bonds link the half-cystinyl residues 26-81, 39-92, and 57-107. The sequence is homologous to that of the pancreatic ribonucleases with 35% identity and many of the remaining residues conservatively replaced. Similarities are especially apparent around the major active-site residues His-12, Lys-41, and His-119 of ribonuclease which are conserved as are three of the four disulfide bonds. The complete chemical characterization of a unique human organogenic messenger molecule, i.e., one that can induce organ formation, accomplishes the first major objective of this long-term investigation of organogenesis in general and angiogenesis in particular. The unexpected homology to ribonuclease suggests novel approaches to the investigation of the biological process of angiogenesis.