PMID: 43739Jan 1, 1978

Further studies on 5'-Nucleotidase from serum of liver cirrhotic individuals

Biochemistry and Experimental Biology
S A Al-Mudhaffar, V Saadalla

Abstract

The kinetic properties of 5'-Nucleotidase were investigated in untreated patients with liver cirrhosis at 37 degrees C. Mg+2 and Mn+2 were found to activate both normal and liver cirrhotic 5'-Nucleotidase, but Nickel inhibited the enzyme in both systems competitively. Both ATP and adenosine act as inhibitors to 5'-Nucleotidase. The inhibitory constant for ATP was different in normal and liver cirrhotic individuals, 0.1 +/- 0.03 for normal and 0.225 +/- 0.02 for liver cirrhosis. In our investigation, ATP was found to be a competitive inhibitor of 5'-Nucleotidase which compete the substrate (A-5'-MP) for the active site. Inhibition of 5'-Nucleotidase by adenosine is of non-competitive type, for both normal and liver cirrhotic sera. It was observed that both serum 5'-Nucleotidase exhibited pH dependent characteristics; in that there was an optimum substrate concentration at each pH value and the plot of pKm versus pH shows great dependency of km on pH.

Related Concepts

Manganese
Nucleotidases
Adenosine
NT5E
Nickel
Fibrosis, Liver
Phosphoglycerate Dehydrogenase Activity
Liver Cirrhosis
Acid phosphatase isoenzyme, prostatic fraction
PHGDH wt Allele

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