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Method of refolding proteins using a dithiol compound a catalyst and a test to determine the potential use of compounds as protein refolding catalyst
Method of refolding proteins using a dithiol compound a catalyst and a test to determine the potential use of compounds as protein refolding catalyst
The use of small molecular weight non-protein dithiol molecules having a pKa of less than about 8.0 and an Eo' of more than about -0.25 V for catalysing the activity of eukaryotic protein folding enzyme protein disulfide isomerase (PDI) and the prokaryotic enzyme thioredoxin. As the exemplary molecule N,N'-bis(2-mercaptoacetyl)-1,2-diaminocyclohexane (BMC), is capable of catalysing the proper formation of disulfide bonds, and the proper folding of proteins, both in vivo and in vitro. This permits a small organic molecule to be substituted for an enzymatic system in protein synthesis.
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