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>>But I see that you mention a theory that they can reduce or eliminate patient antibodies in biologics (relative to conventional methods I presume) - on what basis does this theory exist ?<<
To add to DEW's response, GTCB's claimed niche is the platform to produce "difficult to express" proteins. It is well known that bioreactors and yeast can make accurate amino acid sequences that lack the effectiveness of natural proteins because the glycosylation requires uniquely human enzymes and glycosylation is essential for accurate folding. Glycofi is trying to get around this problem by adding DNA for the human glycosylation enzymes to the yeast genome. Cell culture generally gives an even closer to natural human product. But, the claim of GTCB (which I believe to be true) is that we can fool a goat's udder into producing proteins which are virtually identical to human proteins. As such, they should exhibit full activity. Theoretically, they should also be less immunogenic compared to other methods. Indeed, immunogenicity is a real problem for lab produced recombinant proteins.
So, this is a long way of saying that GTCB does have some theory and evidence to suggest it can produce proteins that are as effective and perhaps no more immunogenic than natural human proteins.
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