The main other way would be to purify the protein from a natural or recombinant source.
Usually natural sources don't have enough purity and yield for most proteins, unless you can find some tissue that expresses a lot of it naturally, like albumin in the blood, or lyoszyme in the egg.
With the recombinant method, you would need to design a gene coding for your protein and transform a suitable host with it, usually E. coli. You could have a tag facilitating purification line hexahistidine. Some of your immune response might be directed against that tag, so that's something to look out for. You don't want to change the sequence too much, or use a protease like TEV to remove the tag. It's a significant project -- You'll need some sort of expertise or collaborator who is good at doing this.
Thanks for your informative answer. What about yeast system? as yeast will excrete the product and the cell disruption process and ease the subsequent purification process.
I would agree with John, yeast system is good for protein expression if the antigen is mainly from an eukaryotic origin. If not the ideal way to express the antigen in high concentration and purity will be recombinant method using the prokaryotic system (e.coli).
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