inosinic-acid has been researched along with Liver-Diseases* in 3 studies
3 other study(ies) available for inosinic-acid and Liver-Diseases
| Article | Year |
|---|---|
Activation energy of serum 5'-nucleotidase as a marker for enzyme heterogeneity.
Using adenosine 5'-monophosphate (Arkesteijn; J. Clin. Chem. Clin. Biochem. 14 (1976) 155) and inosine 5'-monophosphate (Bertrand & Buret; Clin. Chim. Acta 119 (1982) 275) as substrates for the determination of serum 5'-nucleotidase, linear Arrhenius plots were obtained between 25 degrees C and 37 degrees C. With the latter method, in patients with hepatobiliary disease, activation energy is higher than in healthy subjects (67.8 +/- 0.8 kJ.mol-1 vs. 59.2 +/- 1.6 kJ.mol-1, p < 0.001). Neuraminidase treatment resulted in a significant reduction in the activation energy of serum 5'-nucleotidase from patients (63.6 +/- 0.6 kJ.mol-1, p < 0.001). Although the activation energy seen is also influenced by conditions other than sialic acid content, the results obtained are in accordance with the hypothesis that in liver disease serum 5'-nucleotidase becomes more sialylated. Topics: 5'-Nucleotidase; Adenosine Monophosphate; Biliary Tract Diseases; Biomarkers; Enzyme Activation; Humans; Inosine Monophosphate; Kinetics; Liver Diseases; N-Acetylneuraminic Acid; Neuraminidase; Sialic Acids; Thermodynamics | 1994 |
5'-Nucleotidase activity enhanced by manganese and magnesium ions with inosine monophosphate substrate.
Topics: Animals; Humans; Inosine Monophosphate; Liver Diseases; Magnesium; Manganese; Nucleotidases; Rats | 1982 |
A new spectrophotometric method for the determination of 5'-nucleotidase.
A spectrophotometric method is described for the determination of 5'-nucleotidase. In combination with the enzymes nucleoside phosphorylase and xanthine oxidase, inosine, formed by hydrolysis of 5'-IMP by 5'-nucleotidase, is cleaved phosphorolytically to hypoxanthine, which is oxidized to uric acid. In the presence of ethanol, the hydrogen peroxide formed is reduced by catalase and equivalent amounts of acetaldehyde are produced. The aldehyde is dehydrogenated (NADP-dependent) by aldehyde dehydrogenase and the production rate of NADPH is recorded at 334 nm. The inhibition of the unspecific cleavage of 5'-IMP by phosphatases is examined critically. Topics: 5'-Nucleotidase; Aldehyde Oxidoreductases; Alkaline Phosphatase; Bone Diseases; Inosine Monophosphate; Liver Diseases; Nucleotidases; Phosphates; Purine-Nucleoside Phosphorylase; Spectrophotometry, Ultraviolet; Xanthine Oxidase | 1980 |