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		<title>Isolation and characterization of pigeon breast mu...[Acta Biochim Pol. 2005] - PubMed Result
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  <h2>Isolation and characterization of pigeon breast muscle cytosolic 5'-nucleotidase-I (cN-I).</h2>
  <div class="authors"><!--AuthorList--><a href="/sites/entrez?Db=pubmed&amp;Cmd=Search&amp;Term=%22Tkacz-Stachowska%20K%22%5BAuthor%5D&amp;itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_RVAbstractPlus"><b>Tkacz-Stachowska K</b></a>, <a href="/sites/entrez?Db=pubmed&amp;Cmd=Search&amp;Term=%22Lechward%20K%22%5BAuthor%5D&amp;itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_RVAbstractPlus"><b>Lechward K</b></a>, <a href="/sites/entrez?Db=pubmed&amp;Cmd=Search&amp;Term=%22Skladanowski%20AC%22%5BAuthor%5D&amp;itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_RVAbstractPlus"><b>Skladanowski AC</b></a>.</div>
  <p class="affiliation">Department of Molecular Enzymology, Intercollegiate Faculty of Biotechnology UG-MUG, Medical University of Gdańsk, Gdańsk, Poland.</p>
  <p class="abstract">5'-Nucleotidase specific towards dCMP and AMP was isolated from avian breast muscle and characterized. It was found to be similar to a type-I form (cN-I) identified earlier as the AMP-selective 5'-nucleotidase responsible for adenosine formation during ATP breakdown in transfected COS-7 cells. Expression pattern of the cN-I gene in pigeon tissues indicated breast muscle as a rich source of the transcript. We purified the enzyme from this source using two-step chromatography and obtained an active homogenous preparation, free of ecto-5'-nucleotidase activity. The tissue content of the activity was calculated at 0.09 U/g wet weight. The specific activity of the enzyme preparation was 4.33 U/mg protein and it preferred dCMP and AMP to dAMP and IMP as a substrate. Its kinetic properties were very similar to those of the enzyme purified earlier from heart tissue. It was strongly activated by ADP. Inhibition by inorganic phosphate was more pronounced than in heart-isolated cN-I. Despite this difference, a similar physiological function is suggested for cN-I in both types of muscle.</p>
  <p class="pmid">PMID: 15940349 [PubMed - indexed for MEDLINE]</p>
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  <h2>Related articles</h2>
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        <em class="cit">J Biol Chem. 1999 Jun 18; 274(25):17789-93. </em>
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      <p class="note"> [J Biol Chem.  1999]</p>
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      <p class="desc">
        <em class="cit">J Biol Chem. 2000 Apr 21; 275(16):11666-71. </em>
      </p>
      <p class="note"> [J Biol Chem.  2000]</p>
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        <em class="cit">Biochem J. 1990 May 15; 268(1):117-22. </em>
      </p>
      <p class="note"> [Biochem J.  1990]</p>
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      <a href="/pubmed/16770441?ordinalpos=1&amp;itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DiscoveryPanel.Pubmed_Discovery_RA&amp;linkpos=4&amp;log$=relatedreviews&amp;logdbfrom=pubmed"><span class="reviewflag">Review</span>Adenosine as a metabolic regulator of tissue function: production of adenosine by cytoplasmic 5'-nucleotidases.</a>
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        <em class="cit">Acta Biochim Pol. 2006; 53(2):269-78. Epub 2006 Jun 12.</em>
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        <em class="cit">Leuk Lymphoma. 2003 Jul; 44(7):1105-11. </em>
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