High Pressure Refolding of Recombinant Human Growth Hormone from Insoluble Aggregates

High pressure fosters protein refolding from aggregates at high concentrations.

High hydrostatic pressures (1-2 kbar), combined with low, nondenaturing concentrations of guanidine hydrochloride (GdmHCl) foster disaggregation and refolding of denatured and aggregated human growth hormone and lysozyme, and beta-lactamase inclusion bodies. One hundred percent recovery of properly folded protein can be obtained by applying pressures of 2 kbar to suspensions containing aggregat...

Large-scale purification and refolding of recombinant eel growth hormone.

In the past decade, growth hormones (GHs) have been isolated from the pituitaries of several teleost species including tilapia, salmon, carp, and eel.1~9) Although teleost GHs may be useful in promoting growth in aquaculture, little is known about appropriate routes, doses, or patterns of administration. Considerable amounts of teleost GHsare required to clarify both the mode of action of teleo...

Purification of Large Quantities of Biologically Active Recombinant Human Growth Hormone

Production and purification of human growth hormone using a simple method was studied in two recombinantEscherichia coli, D7-5 and C27-2 strains. The r-hGH was expressed in the form of inclusion body in a batchfermentation process and purified to 99% purity using a procedure based on acid precipitation of the hostderived proteins and other impurities. The effect of the pH and ...

Evaluation of Heat Induction Strategy for Recombinant Human Growth Hormone Expression in Fed-Batch Fermentation

An ln vivo Assay for Biological Activity of Synthesized Recombinant Human Growth Hormone