𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Rapid purification and partial characterization of recombinant human epidermal growth factor produced byEscherichia coli

✍ Scribed by V. B. Yadwad; K. Meghji; O. P. Ward

Publisher
Springer-Verlag
Year
1993
Tongue
English
Weight
542 KB
Volume
7
Category
Article
ISSN
0951-208X

No coin nor oath required. For personal study only.

✦ Synopsis

Human recombinant EGF, secreted into the extracellular medium by E. c&i cells, was purified by a combination of solid phase extraction and HPLC. Using these techniques, the peptide was purified 122-fold, with a recovery of greater than 75%. The purified hEGF manifested no contaminating protein bands on electrophoretic gels. Amino acid analysis of the purified peptide was identical to that of authentic hEGF.

πŸ“œ SIMILAR VOLUMES

Characterization and partial purificatio
Characterization and partial purification of human epithelial transforming growth factor
✍ Damien J. Dunnington; Robert G. Scott; Mario A. Anzano; Russell Greig πŸ“‚ Article πŸ“… 1990 πŸ› John Wiley and Sons 🌐 English βš– 907 KB

A polypeptide growth factor has been partially purified from medium conditioned by the human adrenocortical carcinoma cell line SW13. This factor, designated h-TGFe, stimulates anchorage-independent growth of the SW13 cells. Similar activity was observed in human milk, and in conditioned media from

Partial purification and characterizatio
Partial purification and characterization of a growth factor from human hyperplastic prostatic tissues
✍ DignaοΏ½, A. ;Holldorf, A. W. πŸ“‚ Article πŸ“… 1992 πŸ› Springer 🌐 English βš– 565 KB

A growth factor capable of stimulating DNA synthesis of Balb/c 3T3 cells was purified by heparin-Sepharose column chromatography about 1900-fold from the cytosol of human prostatic tissues obtained at autopsy or open prostatectomy. This growth factor bound to heparin-Sepharose in the presence of 0.5