Solubilization of growth hormone and other recombinant proteins from Escherichia coli inclusion bodies by using a cationic surfactant

Recombinant pig growth hormone (rPGH) was solubilized from inclusion bodies by using the cationic surfactant cetyltrimethylammonium chloride (CTAC). The solubilizing action of CTAC appeared to be dependent on the presence of a positively charged head group, as a non-charged variant was inactive. Rel...

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Veröffentlicht in:	Biochemical journal 1992-08, Vol.285 (3), p.871-879
Hauptverfasser:	PURI, N. K, CRIVELLI, E, CARDAMONE, M, FIDDES, R, BERTOLINI, J, NINHAM, B, BRANDON, M. R
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Biological Assay Cell Fractionation Cetrimonium Cetrimonium Compounds Chromatography, High Pressure Liquid Escherichia coli - chemistry Escherichia coli - ultrastructure Fundamental and applied biological sciences. Psychology Growth Hormone - chemistry Growth Hormone - isolation & purification Growth Hormone - pharmacology Growth Plate - drug effects Guanidine Guanidines Insulin-Like Growth Factor II - chemistry Insulin-Like Growth Factor II - isolation & purification Interleukin-1 - chemistry Interleukin-1 - isolation & purification Interleukin-1 - pharmacology Protein Conformation Protein hormones. Growth factors. Cytokines Proteins Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Sheep Solubility Surface-Active Agents Swine Urea
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