Properties of 5'-Nucleotidase from Hepatic Tissue of Higher Animals*
- 1 February 1968
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 63 (2) , 165-169
- https://doi.org/10.1093/oxfordjournals.jbchem.a128757
Abstract
1. 5'-Nucleotidase [EC 3.1.3.5] was partially purified from rat liver acetone powder and it was found to be kinetically distinct from 5'-Nucleotidase which had been reported in rat liver. 2. 5'-IMP and 5'-GMP are the most active substrates among the 5'-mononucleotides tested. 3. This enzyme has optimum pH at 6.5 and requires bivalent metal ions. In the absence of bivalent metal ions, the enzyme is almost inactive. 4. Inosine, guanosine, PCMB and NaF inhibit this enzyme. 5. 5'-Nucleotidase which shows the highest activity with 5'-IMP and 5'-GMP was also obtained from frog and pig liver acetone powder.This publication has 4 references indexed in Scilit:
- 5′-nucleotidase of chicken liverBiochimica et Biophysica Acta (BBA) - Enzymology, 1967
- Subcellular Localization and Properties of 5'-Nucleotidase in the Rat LiverJournal of Biological Chemistry, 1967
- Calf intestinal 5′-nucleotidaseArchives of Biochemistry and Biophysics, 1966
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951