High level expression of soluble angiogenin in Escherichia coli

Human angiogenin was genetically engineered and contained the E. coli Omp A signal sequence for secreting soluble angiogenin to the periplasm under tac promoter control. The angiogenin sequence was encoded in a single gene and expressed as a 14.4 kilodalton soluble protein in E. coli. It was purifie...

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Veröffentlicht in:	Biochemistry and molecular biology international 1999-02, Vol.47 (2), p.267-273
Hauptverfasser:	Yoon, Jong Myung, Kim, Seung Ho, Kwon, Oh Byung, Han, Seung Hee, Kim, Byong Kak
Format:	Artikel
Sprache:	eng
Schlagworte:	angiogenin Bacterial Outer Membrane Proteins - genetics cell‐free translation Chromatography, Affinity Chromatography, Agarose Escherichia coli - genetics Gene Expression Genetic Engineering heparin‐Sepharose Humans Omp A signal sequence Plasmids - genetics Promoter Regions, Genetic Protein Biosynthesis Proteins - genetics Proteins - isolation & purification Recombinant Proteins - isolation & purification Reticulocytes - metabolism Ribonuclease, Pancreatic Solubility
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Beschreibung
Zusammenfassung:	Human angiogenin was genetically engineered and contained the E. coli Omp A signal sequence for secreting soluble angiogenin to the periplasm under tac promoter control. The angiogenin sequence was encoded in a single gene and expressed as a 14.4 kilodalton soluble protein in E. coli. It was purified by CM‐Sepharose ion‐exchange chromatography and by a heparin‐Sepharose affinity chromatography procedure. The biological activity of angiogenin was established by its ability to inhibit mRNA‐dependent rabbit reticulocyte cell‐free translation.
ISSN:	1521-6543 1039-9712 1521-6551
DOI:	10.1080/15216549900201283