RESUMEN
Results of examination and treatment of 157 patients with cholelithiasis against the background of a liver pathology were summed up. The antioxidant system in such patients was studied. The degree of a decrease of catalase activity in the liver and blood serum as well as the ascorbic acid content were found to depend on the liver state of patients with cholelithiasis. Greatest changes were found in patients with cirrhosis of the liver and chronic active hepatitis. The method of complex treatment of cholelithiasis patients with non-enzymatic antioxidants alpha-tocopherol and ascorbic acid is proposed. Activity of organ specific liver enzymes urokaninase and histidase was used for the estimation of treatment efficiency. Complex administration of ascorbic acid and alpha-tocopherol was shown to improve the liver function in patients operated upon for cholelithiasis.
Asunto(s)
Antioxidantes/uso terapéutico , Colelitiasis/terapia , Ácido Ascórbico/análisis , Bilis/química , Bilis/enzimología , Biopsia , Catalasa/análisis , Colelitiasis/metabolismo , Terapia Combinada , Hepatitis Crónica/metabolismo , Hepatitis Crónica/terapia , Histidina Amoníaco-Liasa/análisis , Humanos , Hígado/química , Hígado/enzimología , Hígado/patología , Cirrosis Hepática/metabolismo , Cirrosis Hepática/terapia , Urocanato Hidratasa/análisisAsunto(s)
Hidroliasas/análisis , Hígado/enzimología , Urocanato Hidratasa/análisis , Animales , Bovinos , Activación Enzimática , Femenino , MétodosRESUMEN
Urocanase (urocanate hydratase, EC 4.2.1.49) purified from Pseudomonas testosteroni has a mol.wt. of 118000 determined by sedimentation-equilibrium analysis. Ultracentrifugation in 6M-guanidine hydrochloride and polyacrylamide-gel electrophoresis in sodium dodecyl sulphate show that the enzyme consists of two identical or very similar subunits. It is, like urocanase isolated from other sources, inhibited by reagents that react with carbonyl groups. Although urocanase from Ps. testosteroni is strongly inhibited by NaBH4, no evidence could be obtained for the presence of covalently bound 2-oxobutyrate as a prosthetic group; this is in contrast with findings elsewhere for urocanase from Pseudomonas putida. Urocanase from Ps. testosteroni does not contain pyridoxal 5'-phosphate as a coenzyme and in this respect is similar to all urocanases studied in purified form.
Asunto(s)
Hidroliasas/análisis , Pseudomonas/enzimología , Urocanato Hidratasa/análisis , Borohidruros , Centrifugación por Gradiente de Densidad , Fenómenos Químicos , Química , Hidroxibutiratos/análisis , Cinética , Peso Molecular , Piridoxal/análogos & derivados , Piridoxal/análisis , Urocanato Hidratasa/antagonistas & inhibidores , Urocanato Hidratasa/aislamiento & purificaciónRESUMEN
A mutation of Salmonella typhimurium was obtained that results in the failure of cells to synthesize the enzyme l-histidine ammonia-lyase (histidase). The mutation mapped within the hutH gene and in merodiploid strains was dominant over the wild-type allele. Extracts from cells bearing the trans-dominant histidase-negative allele were shown to contain material that reacts immunologically with antiserum against purified wild-type histidase. It is proposed that the trans-dominant allele results in the synthesis of defective histidase subunits that can combine with, and partially inactivate, wild-type histidase subunits. This subunit mixing presumably does occur, as the enzyme synthesized in a hybrid merodiploid strain is abnormally heat sensitive.