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Alias Born 06/05/2007

Re: Pre_Clinical post# 4258

Monday, 07/23/2007 6:20:38 PM

Monday, July 23, 2007 6:20:38 PM

Post# of 19309
I don't think there is any good information in this regard.

The glycosylation pattern is different in the goats. For Atryn this does not appear to impinge on its function as the EMEA trial demonstrated for the surgery patients.

As to whether or not this will effect the function of ALL the products of goat production system is an unknown. This will have to be evaluated on a case by case basis as it is for every recombinant protein. If one cares to speculate I would say that its an advantage to have some mammalian like glycosylation over cell systems which do not yield any glycosylated protein.

Certainly it has been shown that many entirely non-glycosylated versions of proteins which normally are glycosylated work just find in therapeutic applications. This is not to say that they all have as we only hear about those that do work.

While we are on this line of thought:
Has it been shown by GlycoFi that their glycosylated proteins produced in the modified yeast are identical to their human counterparts?

Do they act identically?
DAK

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