Confirmation that catalase is a glycoprotein.
Catalases which had been purified from the livers of mouse, rat and guinea pig were subjected to mild periodate oxidation followed by reduction with sodium boro[3H]hydride in order to test for the presence of sialic acid. A radioactively labelled moiety resulted, which behaved as a derivative of N-acetyl neuraminic acid during mild acid hydrolysis, neuraminidase treatment, ion exchange chromatography and paper chromatography. It is concluded that mammalian catalases are glycoproteins, and possess variable amounts of N-acetyl neuraminic acid in their carbohydrate moiety.
D000818:Animals; D001894:Borohydrides; D002374:Catalase / Q000302:isolation & purification*; D006023:Glycoproteins / Q000302:isolation & purification*; D006168:Guinea Pigs; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology*; D051379:Mice; D019158:N-Acetylneuraminic Acid; D010084:Oxidation-Reduction; D010504:Periodic Acid; D051381:Rats; D012794:Sialic Acids / Q000032:analysis; D013045:Species Specificity
D001894:Borohydrides; D006023:Glycoproteins; D012794:Sialic Acids; D010504:Periodic Acid; D002374:Catalase; D019158:N-Acetylneuraminic Acid