Isolation and characterization of angiogenin, an angiogenic protein from human carcinoma cells

Biochemistry. 1985 Sep 24;24(20):5480-6. doi: 10.1021/bi00341a030.


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 approximately 0.5 microgram/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 greater than 9.5), single-chain protein of molecular weight approximately 14 400 has been determined. The amino terminus is blocked, and the carboxyl-terminal residue is proline.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenocarcinoma / analysis*
  • Allantois / drug effects
  • Amino Acid Sequence
  • Amino Acids / analysis
  • Angiogenesis Inducing Agents / isolation & purification*
  • Angiogenesis Inducing Agents / pharmacology
  • Animals
  • Biological Assay
  • Cell Line
  • Chick Embryo
  • Chorion / drug effects
  • Colonic Neoplasms / analysis*
  • Culture Media
  • Growth Substances / isolation & purification*
  • Humans
  • Molecular Weight
  • Neoplasm Proteins / isolation & purification*
  • Ribonuclease, Pancreatic*


  • Amino Acids
  • Angiogenesis Inducing Agents
  • Culture Media
  • Growth Substances
  • Neoplasm Proteins
  • angiogenin
  • Ribonuclease, Pancreatic