Placenta
Volume 31, Issue 5 , Pages 460-462 , May 2010

AMP-Deaminase from Developing Human Placenta

  • A. Swieca

      Affiliations

    • Department of Biochemistry and Clinical Physiology, Medical University of Gdansk, Debinki 1, 80-211 Gdansk, Poland
  • ,
  • I. Rybakowska

      Affiliations

    • Department of Biochemistry and Clinical Physiology, Medical University of Gdansk, Debinki 1, 80-211 Gdansk, Poland
    • Corresponding Author InformationCorresponding author. Tel./fax: +48 58 349 14 65.
  • ,
  • R. Milczarek

      Affiliations

    • Department of Pharmaceutical Biochemistry, Medical University of Gdansk, Debinki 1, 80-211 Gdansk, Poland
  • ,
  • J. Klimek

      Affiliations

    • Department of Pharmaceutical Biochemistry, Medical University of Gdansk, Debinki 1, 80-211 Gdansk, Poland
  • ,
  • K. Kaletha

      Affiliations

    • Department of Biochemistry and Clinical Physiology, Medical University of Gdansk, Debinki 1, 80-211 Gdansk, Poland

,Accepted 12 February 2010.

References 

  1. Chapman AG, Atkinson DE. Stabilization of the adenylate energy charge by the adenylate deaminase reaction. J Biol Chem. 1973;248:8309–8312
  2. Weber G. Enzymes of purine metabolism in cancer. Clin Biochem. 1983;16:57–63
  3. Ogasawara N, Goto H, Yamada Y, Watanabe T, Asano T. AMP deaminase isozymes in human tissues. Biochim Biophys Acta. 1982;714:298–306
  4. Marquetant R, Desai NM, Sabina RL, Holmes EW. Evidence for sequential expression of multiple AMP deaminase isoforms during skeletal muscle development. Proc Natl Acad Sci USA. 1987;84:2345–2349
  5. Kaletha K, Nowak G. Developmental form of human skeletal-muscle AMP deaminase. The kinetic and regulatory properties of the enzyme. Biochem J. 1988;249:255–261
  6. Morisaki T, Sabina RL, Holmes EW. Adenylate deaminase. A Multigene family in humans and rats. J Biol Chem. 1990;265:11482–11486
  7. Makarewicz W, Mackowiak E. Adenosine-5′-monophosphate aminohydrolase of human placenta. Acta Biochim Pol. 1971;18:135–142
  8. Makarewicz W. Purification and properties of AMP-aminohydrolase from human placenta. Acta Biochim Polon. 1974;21:125–135
  9. Swieca A, Rybakowska I, Nagel-Starczynowska G, Kossowska E, Kaletha K. AMP-deaminase from human term placenta. Mol Cell Biochem. 2003;252:363–367
  10. Roszkowska A, Klimek J, Kaletha K. Expression patterns of AMP-deaminase and cytosolic 5′-nucleotidase genes in human term placenta. Mol Cell Biochem. 2008;311:249–251
  11. Chaney AL, Marbach EP. Modified reagents for determination of urea and ammonia. Clin Chem. 1962;8:130–132
  12. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal Biochem. 1976;72:248–254
  13. Szydłowska M, Roszkowska A. Expression patterns of AMP-deaminase isozymes in human hepatocellular carcinoma (HCC). Mol Cell Biochem. 2008;318:1–5
  14. Remesar X, Arola L, Palou A, Alemany M. Activities of enzymes involved in Amino-acid metabolism in developing rat placenta. Eur J Biochem. 1980;110:289–293
  15. Szydłowska M, Nagel-Starczynowska G, Rybakowska I, Swieca A, Kaletha K. Human liver AMP-deaminase – oligomeric forms of the enzyme. Mol Cell Biochem. 2002;241:81–86
  16. Szydłowska M, Chodorowski Z, Rybakowska I, Nagel-Starczynowska G, Kaletha K. Full-size form of human liver AMP-deaminase?. Mol Cell Biochem. 2004;266:133–137

PII: S0143-4004(10)00088-3

doi: 10.1016/j.placenta.2010.02.009

Placenta
Volume 31, Issue 5 , Pages 460-462 , May 2010