Abstract

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.

Keywords

AngiogeninIsoelectric pointChorioallantoic membraneAmino acidIn vivoBiochemistryChemistryCell cultureIsoelectric focusingProlineBiologyEndostatinMolecular biologyAngiogenesisIn vitro

MeSH Terms

AdenocarcinomaAllantoisAmino Acid SequenceAmino AcidsAngiogenesis Inducing AgentsAnimalsBiological AssayCell LineChick EmbryoChorionColonic NeoplasmsCulture MediaGrowth SubstancesHumansMolecular WeightNeoplasm ProteinsRibonucleasePancreatic

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Publication Info

Year
1985
Type
article
Volume
24
Issue
20
Pages
5480-5486
Citations
912
Access
Closed

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912
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Cite This

James W. Fett, Daniël J. Strydom, Roy R. Lobb et al. (1985). Isolation and characterization of angiogenin, an angiogenic protein from human carcinoma cells. Biochemistry , 24 (20) , 5480-5486. https://doi.org/10.1021/bi00341a030

Identifiers

DOI
10.1021/bi00341a030
PMID
4074709

Data Quality

Data completeness: 81%