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
β¦ LIBER β¦
Purification and characterization of recombinant bovine growth hormone produced in Escherichia coli
β Scribed by Jang Won Choi; Sung II Kim; Se Yong Lee
- Book ID
- 110222855
- Publisher
- Springer Netherlands
- Year
- 1998
- Tongue
- English
- Weight
- 911 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0141-5492
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Rapid purification and partial character
β
V. B. Yadwad; K. Meghji; O. P. Ward
π
Article
π
1993
π
Springer-Verlag
π
English
β 542 KB
Purification and structural characteriza
β
Chun-Yen Lai; Elizabeth Dharm; Yutaka Fujii
π
Article
π
1989
π
Elsevier Science
π
English
β 716 KB
Purification and characterization of a S
β
Biedermann, Kirsten; Jepsen, Pia Knak; Riise, Erik; Svendsen, Ib
π
Article
π
1989
π
Springer-Verlag
β 778 KB
Renaturation, purification, and characte
β
A. Agraz; J. Paulsen; B. BΓΆrner; H. Hustedt
π
Article
π
1995
π
Elsevier Science
π
English
β 689 KB
Enhanced expression of bovine growth hor
β
Jang Won Choi; Se Yong Lee
π
Article
π
1997
π
Springer Netherlands
π
English
β 538 KB
Recombinant production and purification
Recombinant production and purification of novel antisense antimicrobial peptide in Escherichia coli
β
Chris Haught; Gregory D. Davis; Rajesh Subramanian; Ken W. Jackson; Roger G. Har
π
Article
π
1998
π
John Wiley and Sons
π
English
β 330 KB
π 2 views
A fusion protein was genetically engineered that contains an antimicrobial peptide, designated P2, at its carboxy terminus and bovine prochymosin at its amino terminus. Bovine prochymosin was chosen as the fusion partner because of its complete insolubility in Escherichia coli, a property utilized t