Journal
CHEMICAL COMMUNICATIONS
Volume 53, Issue 76, Pages 10600-10603Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7cc05888h
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The selective hydrolysis of the glycosidic bond between the terminal sialic acid and the penultimate sugar has been achieved in the alpha-2-HS-glycoprotein (Fetuin-A) in the presence of H3PW12O40, a Keggin type polyoxometalate. A controlled liberation of sialic acid from the glycoprotein could be achieved at pH 3.0 and 37 degrees C without the destruction of the protein backbone.
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