Horm Metab Res 1999; 31(1): 5-7
DOI: 10.1055/s-2007-978687
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Decreased Na,K-ATPase Activity by Glycation at the Catalytic Center

T. Katori1 , C. Bannai1 , Y. Hayashi2 , K. Yamashita1
  • 1Division of Endocrinology and Metabolism, Institute of Clinical Medicine, University of Tsukuba, Tsukuba, Ibaraki, Japan
  • 21st Department of Biochemistry, Kyorin University School of Medicine, Mitaka, Tokyo, Japan
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Publication History



Publication Date:
19 April 2007 (online)

The in vitro activity of Na,K-ATPase isolated from outer medulla of dog kidney was decreased in a dose- and time-dependent manner by interaction with 100 mM glucose 6-phosphate (G6P) during the first 8 h. In the subsequent 16 h no change in activity was observed. On the other hand, Amadori-products of the enzyme increased in a dose- and time-dependent manner by glycation up to 100 mM G6P during 24 h. The presence of 5 mM ATP in glycation experiments protected the enzyme activity but did not inhibit the formation of Amadori-products. These results were consistent with inhibition of the Na,K-ATPase activity by glycation of the amino groups located in the catalytic center of the molecule.