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PubMedDate not supplied

[Phenylalanine-4-hydroxylase activity in the liver in viral hepatitis].

Phenylalanine-4-hydroxylase activity was studied in liver tissue, obtained by biopsy from 5 patients with viral hepatitis and from 8 persons without parthological alterations of liver. The enzymatic activity was estimated by formation of 14C-tyrosine in presence and in absence of added cofactor 2-amine-4-hydroxy-6,7-dimethyltetrahydropteridine. Without addition of the cofactor the phenylalanine hydroxylase activity was of the same order of magnitude in liver tissue of the patients and of healthy persons. In presence of the cofactor the enzyme activity in liver of the patients with the hepatitis of moderate severity constituted 44% of the activity found in the control group. The rate of phenylalanine hydroxylation was 0.19 with 10-2 min-1 in patients with hepatitis and 0.5 with 10-2 min-1--in the control group. In severe and moderate forms of viral hepatitis the impairment of phenylalanine metabolism was due to decrease in the activity of phenylalanine-4-hydroxylase in liver tissue.

Biopsy↗
PubMed1984

[Substitution of antithrombin III by synthetic thrombin inhibitors].

Synthetic, low-molecular weight thrombin inhibitors may substitute for antithrombin III in inactivating thrombin in vitro and in vivo. They are superior to heparin as antithrombotic agents in antithrombin deficiency or consumption. Studies in experimental animals show the effectiveness of synthetic thrombin inhibitors in immunologic antithrombin depletion, thrombin-induced consumption and CCl4-induced liver failure.

Animals↗
PubMedDate not supplied

NADH-coupled spectrophotometric assay of tyrosine aminotransferase.

A rapid spectrophotometric method for estimation of tyrosine aminotransferase activity (TAT) is described, based on a coupled reaction with NADH-dependent aromatic ketoacid reductase. 3-iodo-L-tyrosine, upon TAT action, is transformed into 3-iodo-4-hydroxyphenylpyruvate which quickly reacts with NADH in the presence of aromatic ketoacid reductase; oxidation rates at 340 nm are linear with protein concentration over the whole range of purification steps of TAT. This new method, for its sensitivity, easy performance and possibility of a continuous monitoring of TAT reaction, may be considered comparable to the more diffuse spectrophotometric standard method, and also as an alternative, advantageous procedure in some instances. The method for purification of the coupled aromatic ketoacid reductase is also described.

Alcohol Oxidoreductases↗