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Enzyme pp 711-717 | Cite as

Mutarotase

5.1.3.3 Aldose l-epimerase
  • Albert S. Keston
Chapter
Part of the Handbuch der Physiologisch- und Pathologisch-Chemischen Analyse book series (HOPPE-SEYLER)

Zusammenfassung

Bentley and Neuberger 1 presented evidence in 1949 for the existence of a catalyst possessing mutarotational activity for glucose in glucose oxidase (notatin) preparations. In the examination of two purified samples of notatin, Keilin and Hartree 2 found that while the activity against equilibrium glucose was virtually the same, the activity against a-glucose was much higher for one of the preparations. This difference was ascribed to the presence of a mutarotational catalyst unrelated to glucose oxidase activity. Keston 3 found mutarotase in various animal tissues. Kidneys of animals which reabsorb glucose in large amounts contain largest amounts of this enzyme4–6 while the kidneys of aglomerular fish5–7, which do not reabsorb glucose, contain very little mutarotase. Kidney cortex contains more of the enzyme than the medulla1–2. Retina, brain, tumor tissue3–5 and intestine6–8 also have considerable amounts of the enzyme. The enzyme is reported to be distributed mainly in the mucosa of the intestine2. In general, the amount of mutarotase present correlates with the amount of transport of glucose (kidneys) or glycolysis (other tissues)3–5. Keston has proposed a unitary theory of glucose transport and reabsorption based on mutarotase9.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1967

Authors and Affiliations

  • Albert S. Keston
    • 1
  1. 1.Institute for Medical Research and StudiesNew York 1N. Y.USA

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