Table 1 Results of culturing, isolation of inclusion bodies, and chromatographic purification of hGH from E. coli DH5α cells carrying the pIGDMKUH plasmid
From: Use of Ubp1 protease analog to produce recombinant human growth hormone in Escherichia coli
Phase – Ub/hGH | Volume (ml) | Protein | |||
|---|---|---|---|---|---|
(mg/ml) | (mg) (%) | ||||
Dissolved inclusion bodies | 200 | 2.2 | 443.3 (100) | ||
DEAE | Column entry | 200 | 2.2 | 443.3 (100) | |
Sepharose | |||||
Fast Flow | Fraction | 184 | 1.32 | 242.8 (54.7) | |
Column | |||||
SP | Column entry | 184 | 1.32 | 242.8 (54.7) | |
Sepharose | |||||
Fast Flow | Fraction | 184 | 1.25 | 230 (51.8) | |
Column | |||||
Protein after renaturation | 1680 | 0.14 | 230 (51.8) | ||
Protein after ammonium sulfate precipitation to 80% saturation | 50 | 2.85 | 142.5 (32.1) | ||
Phase – hGH | Volume (ml) | Protein | HPLC purity (%) | ||
(mg/ml) | (mg) (%) | ||||
Phenyl | Column entry | 64 | 1.73 | 110.7 (24.9) | 50 |
Sepharose | |||||
Fast Flow | Fractions | 50 | 0.85 | 42.4 (9.56) | 91.8 |
Column | |||||
Q | Column load | 50 | 0.85 | 42.4 (9.56) | 91.8 |
Sepharose | |||||
Fast Flow | Fractions | 10 | 4.02 | 40.2 (9.06) | 92.2 |
Column | |||||