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- W1995883105 abstract "Abstract The enzyme mutarotase was found in lysed human erythrocytes and in hemoglobin. It was separated from hemoglobin and partially purified by treatment with ethanol and chloroform at —15 °. The enzyme prepared from equine hemoglobin had an average K m of 0.061 m as determined by a dialysis-coupled enzyme method and a conventional polarimetric method. It was nondialyzable, heat-sensitive, and was strongly inhibited by d -galactose, l -arabinose, d -ribose, d -xylose, and d -arabinose, but only slightly by d -fructose, lactose, and d -maltose, and not at all by sucrose. Hemoglobin preparations from five different species of mammals indicated some striking differences in mutarotase activity. The existence of mutarotase and its properties in erythrocytes may suggest a relationship to sugar penetration into red blood cells, and/or even some function in carbohydrate metabolism and transport in the body." @default.
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- W1995883105 date "1968-03-01" @default.
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- W1995883105 title "Isolation and properties of mutarotase in erythrocytes" @default.
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- W1995883105 doi "https://doi.org/10.1016/0003-9861(68)90172-0" @default.
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