Literature DB >> 1148256

5'-nucleotidase: an ecto-enzyme of frog skeletal muscle.

Y T Woo, J F Manery.   

Abstract

Using 1-4C-labeled AMP and IMP as substrates, 5'-nucleotidase (5'-ribonucleotide phosphohydrolase, EC 3.1.3.5) activity was detected at the external surface of frog skeletal muscle with the active site facing toward the extracellular space. The enzyme was firmly bound to the muscle membrane. Its activity was dependent on Ca2+ or Mg2+ and was inhibited by non-radioactive ribonucleoside 5'-monophosphates, or theophylline, while adenosine 3'-monophosphate and p-nitrophenylphosphate had little or no effect. 5'-Nucleotidase with similar properties was also found in the isolated plasma membrane fraction of the muscle.

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Year:  1975        PMID: 1148256     DOI: 10.1016/0005-2744(75)90188-6

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

Review 1.  Extracellular ATP: effects, sources and fate.

Authors:  J L Gordon
Journal:  Biochem J       Date:  1986-01-15       Impact factor: 3.857

2.  Further studies on a unique T-tubular acid phosphatase in avian skeletal muscle.

Authors:  J J Trout; W T Stauber; B A Schottelius
Journal:  Histochem J       Date:  1981-05

3.  A kinetic study of the soluble 5'-nucleotidase of rat liver.

Authors:  G van den Berghe; C van Pottelsberghe; H G Hers
Journal:  Biochem J       Date:  1977-03-15       Impact factor: 3.857

4.  Effects of adenosine 5'-triphosphate (ATP) and beta-gamma-methylene ATP on the rat urinary bladder.

Authors:  C Brown; G Burnstock; T Cocks
Journal:  Br J Pharmacol       Date:  1979-01       Impact factor: 8.739

  4 in total

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