AI Article Synopsis
- Recombinant mutant human granulocyte colony stimulating factor (rmhG-CSF) was engineered by mutating specific amino acids and adding a cysteine residue at the C-terminal.
- The modified rmhG-CSF was pegylated using a PEG-Mal 20000 compound and purified through ion-exchange and gel filtration chromatography, achieving over 95% purity as confirmed by SDS-PAGE analysis.
- Bioactivity studies demonstrated that the pegylated rmhG-CSF maintained its full functionality and had a longer half-life in mice compared to traditional pegylation methods.
Article 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.
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