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FEBS Lett ; 528(1-3): 257-60, 2002 Sep 25.
Article in English | MEDLINE | ID: mdl-12297316

ABSTRACT

Human growth hormone (hGH), whose main function is the somatic growth stimulation, induces diverse effects including lactation. We examined the possibility of hGH stabilization by elimination of its lactogenic activity. Chimeric GHs were constructed by replacement of different segments of hGH with sequences derived from non-lactogenic porcine GH. As was observed in the rat Nb2-11C lymphoma cell test, lactogenic activity of some chimeric hormones was seriously destroyed. This kind of hormones displayed the substantial increase in thermal and guanidine hydrochloride stability. The more stable hGH variants were found to be more soluble in Escherichia coli cells.


Subject(s)
Human Growth Hormone/chemistry , Animals , Cell Line , Drug Stability , Escherichia coli/genetics , Escherichia coli/metabolism , Female , Growth Hormone/chemistry , Growth Hormone/genetics , Growth Hormone/pharmacology , Guanidine , Hot Temperature , Human Growth Hormone/genetics , Human Growth Hormone/pharmacology , Humans , In Vitro Techniques , Inclusion Bodies/metabolism , Lactation/drug effects , Protein Denaturation , Protein Structure, Secondary , Rats , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/pharmacology , Solubility , Swine
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