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Re: DragonBits post# 9330

Wednesday, 03/19/2008 9:12:26 PM

Wednesday, March 19, 2008 9:12:26 PM

Post# of 19309
We have known about Glycofi for quite some time and you are far too kind towards them and optimistic about them as if they are ready to complete with GTCB. Don't just believe thier press releases. All they have done is to place the human glycosylation enzymes into yeast. While it is an very impressive accomplishment, as Jesse says, glycolyslation is only a part of the battle. There are a large number of protein chaperones in cells, which bind top and fold proteins in an orderly fashion. Many of these are associated with nascent proteins as they are being translated, which helps ensure that the proteins folds in a proper way so that they are stable and functional.

Glycosylation and chaperones also serve to allow the proteins to be moved along the secretory pathway, and for proper folding and even proteolytic cleavage, as part of the targeting mechanism to the appropriate intracellular compartment. Different glycosylations serve primarily to transit the proteins in a pathway from ER surface, to ER lumen, to inner and outer golgi to secretory vessicles, which could lead to its ultimate secretion into the extracellular media. Failure to properly execute any step could cause you to make a alot of worthless non-functional proteins that could still be properly gycoslyated. The advantage of mammary glands is they are designed as secretory machines.

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