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J. Biochem, 1968, Vol. 63, No. 2 165-169
© 1968 Japanese Biochemical Society

research-article

Properties of 5'-Nucleotidase from Hepatic Tissue of Higher Animals*

ROICHI ITOH, AKIRA MITSUI and KEIZO TSUSHIMA

From the Department of Biochemistry, Yokohama City University, School of Medicine Yokohama

1. 5'-Nucleotidase [EC 3.1.3.5 [EC] ] 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.

* Dedicated to Dr. Koozoo Kaziro, Professor Emeritus of the Nippon Medical School, on the occasion of his 70th birthday.


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