Conformation growth hormone

D. N. Brems, Solubility of different folding conformers of bovine growth hormone, Biochemistry, 27, 44541 (1988). 

M. Deber, M. K. Lutek, E. P. Heimer and A. M. Felix, Conformational origin of a difficult coupling in a human growth hormone releasing factor analog, Peptide Res., 1989,2, 184-188. 

This disease develops when an abnormal prion protein present in the cadaveric material induces a cascade of conformational changes in host protein. Creutzfeldt-Jakob disease in recipients of somatropin differs from the sporadic form, in that it usually presents with cerebellar signs rather than cognitive impairment, and also in the prominence of prion protein amyloid plaques in nervous tissue (18). In a review, 139 cases of Creutzfeldt-Jakob disease were identified worldwide in people treated with cadaveric somatropin before recombinant human growth hormone became available in the mid-1980s (19). The prevalence of this fatal neurodegenerative condition in recipients of somatropin ranges from 0.3% in the USA to 4.4% in France. Creutzfeldt-Jakob disease has been reported to start at 4-30 years after therapy with cadaveric somatropin (18), so that further cases are anticipated and continue to be reported (20). 

P. Oroszlan, S. Wicar, G. Teshima, S.-L. Wu, W. S. Hancock, and B. L. Karger, Conformational effects in the reversed-phase chromatographic behavior of recombinant human growth hormone and N-methionyl recombinant growth hormone, Anal. Chem., 64 1623 (1992). 

COLUMN STABILITY. The absence of a porous support structure results in enhanced column stability at elevated temperature and pH even with micropellicular sorbents prepared from siliceous supports (14). This is illustrated by the chromatogram in Figure 5 which shows the separation of minor conformers of human growth hormone by using a moderately alkaline mobile phase (pH 8.5). Prior to obtaining the above chromatogram, the column was perfused with 4000 column volumes of the mobile phase at 80°C, yet no noticeable changes in retention behavior, separation efficiency and sample recovery had been observed with respect to initial column performance. 

Hovorka SW, Hong J, Cleland JL, and Schoneich C. Metal-Catalyzed Oxidation of Human Growth Hormone Modulation by Solvent-Induced Changes of Protein Conformation.2001 90 58—69. 

Sukumar M, Storms, SM, and De Felippis, MR. Non-native Intermediate Conformational States of Human Growth Hormone in the Presence of Organic Solvents. Pharm Res 2005 22 789-796. 

Kasimova MR, Milstein SJ, Freire E. The conformational equilibrium of human growth hormone. J Mol Biol 1998 277(2) 409 18. 

In a project implemented at Nil, ovine growth hormone (oGH) was expressed as inclusion bodies using a pQE expression vector. The expressed protein was 10 -15% of the total cellular proteins of E. coli. The recombinant ovine growth hormone was purified from inclusion bodies and refolded into its native conformation. The refolded recombinant oGH was found to be immunoreactive with RIA/RRA characterized by SDS-PAGE, Western blot, N-terminal amino acid sequence, CD, fluorescence spectra, RIA, and RRA. High cell density cultivation was standardized and found to be enhanced to 100 times. In 16 h, 3.2 g H of oGH was produced which is claimed to be the highest level of any recombinant growth hormone reported in E. coli [57]. 

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