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Full-size form of human liver AMP-deaminase?

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Abstract

AMP-deaminase from human liver was purified by two-step phosphocellulose chromatography, and SDS-PAG electrophoresis of the most active enzyme fraction eluted has been performed. The largest of the protein fragments revealed had a size (92 kDa) of an apparent full-size enzyme subunit, and reacted positively with antibodies produced against specific human ampd2 gene product. Three-day storage at cold room temperature modified significantly the electrophoretical pattern of the enzyme, evidencing continuous and progressive degradation of its structure. This is a first report evidencing the presence of apparent full-size form of human liver AMP-deaminase in preparation obtained from endogenous source (Mol Cell Biochem 266: 133–137, 2004)

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Authors and Affiliations

  1. Department of Biochemistry, Medical University of Gdansk, Debinki, Gdansk, Poland.

    M. Szydlowska, I. Rybakowska & K. Kaletha

  2. I Clinic of Internal Medicine and Toxicology, Medical University of Gdansk, Debinki, Gdansk, Poland

    Z. Chodorowski

  3. Department of Pharmaceutical Biochemistry, Medical University of Gdansk, Debinski, Poland

    G. Nagel-Starczynowska

Authors
  1. M. Szydlowska
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  2. Z. Chodorowski
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  3. I. Rybakowska
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  4. G. Nagel-Starczynowska
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  5. K. Kaletha
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Szydlowska, M., Chodorowski, Z., Rybakowska, I. et al. Full-size form of human liver AMP-deaminase?. Mol Cell Biochem 266, 133–137 (2004). https://doi.org/10.1023/B:MCBI.0000049150.19623.e8

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  • DOI: https://doi.org/10.1023/B:MCBI.0000049150.19623.e8

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