Recombinant Human Growth Hormone-Binding Protein Fails to Enhance the in Vivo Bioactivity of Human Growth Hormone in Normal Rats

Recombinant human growth hormone-binding protein fails to enhance the in vivo bioactivity of human growth hormone in normal rats.

GH circulates in the plasma partially bound with a GH-binding protein (GHBP), but the physiological significance of the GHBP and how it affects GH bioactivity in vivo is still unknown. In the present study, we took advantage of the known biological action of exogenous human (h) GH to inhibit endogenous rat (r) pulsatile GH release and examined the effect of combining hGH with recombinant hGHBP ...

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

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

A Microcalorimetry Study of the Binding of Nickel Ion by Human Growth Hormone

A binding study of nickel ions by a new recombinant human Growth Hormone (hGH), produced as an injected drug, has been done at 27˚C in NaCl solution (50 mM) using an isothermal titration calorimetry. There is a set of three identical and non-interacting binding sites for nickel ions. The intrinsic dissociation equilibrium constant and the molar enthalpy of binding are 40 μM and -16...

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 ...