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Chinese Journal of Biotechnology ; (12): 919-923, 2007.
Article in Chinese | WPRIM | ID: wpr-276186

ABSTRACT

Recombinant mutant human granulocyte colony stimulating factor (rmhG-CSF) was pegylated, purified and characterized. rhG-CSF was mutated in position 1,3,4,5,17, and cysteine was added in C-terminal. rmhG-CSF was pegylated by PEG-Mal 20000 and separated by ion-exchange chromatography, gel filtration chromatography. Analysis of SDS-PAGE showed thar the purity of the separated PEG-rmhG-CSF was greater than 95%. and in intro and in vivo bioactivity study showed that target modified PEG-rmhG-CSF kept full bioactivity which was better than traditional pegylation method, and longer half-life was proved in mice.


Subject(s)
Humans , Amino Acid Sequence , Base Sequence , Chromatography, Ion Exchange , Granulocyte Colony-Stimulating Factor , Chemistry , Genetics , Molecular Sequence Data , Mutant Proteins , Genetics , Polyethylene Glycols , Chemistry , Protein Sorting Signals , Recombinant Proteins
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