Abstract

Abstract S -Methylthioacetimidate is a novel amidation reagent which can be used even as low as pH 5 without any side of reaction or crosslinking of the protein. At pH 6, a complete modification of all accessible lysines of bovine serum albumin, pig heart lactate dehydrogenase and glucose dehydrogenase from Bacillus megaterium could be achieved by a single addition of reagent. The protection of the essential lysine of glucose dehydrogenase ( B . megaterium ) was significantly improved when using thioacetimidate at pH 6.0 instead of the O -acetimidate at pH 8.5. The residual activity was 70% with the thiomidate in contrast to 10% with the normally used )-acetimidate.

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