Mutarotase in erythrocytes: isolation and properties.
Mutarotase was found in lysed human erythrocytes and in hemoglobin. The enzyme was partially purified by treatment with ethanol and chloroform at -15 degrees C. It was nondialyzable and heat sensitive, and was inhibited by D-galactose, L-arabinose, D-ribose, D-xylose, and D-arabinose.
D001089:Arabinose; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002725:Chloroform; D004492:Edetic Acid; D004912:Erythrocytes / Q000201:enzymology*; D000431:Ethanol; D005690:Galactose; D006454:Hemoglobins; D006801:Humans; D007535:Isomerases / Q000037:antagonists & inhibitors / Q000097:blood*; D007700:Kinetics; D012266:Ribose; D014994:Xylose
D006454:Hemoglobins; D000431:Ethanol; D012266:Ribose; D002725:Chloroform; D004492:Edetic Acid; D014994:Xylose; D001089:Arabinose; D007535:Isomerases; D005690:Galactose