glutaminase/hepatitis

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[Influence of partial hepatectomie on ammoniumdetoxications function of liver at chronic tetrachlorcarbon hepatitis].

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The purpose. To study the effect of partial hepatectomy (PH) on the main ways of ammonia detoxication in the liver (synthesis of urea and glutamine) in chronic tetrachlorcarbon (CCl4) hepatitis. Methods. The experiments were performed on 165 white outbred rats (females) weighing 180-220 g Chronic

[The ammonia neutralization function of the liver in chronic active hepatitis].

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In experiments on 182 white male rats hepatitis was modelled by percutaneous injection of 0.1 ml/500 g of tetrachloromethane (TCM) dissolved in olive oil. TCM was injected every other day for 65 days. After development of hepatitis (in 65 days) synthesis of glutamine and urea, partial oxygen

Phosphate-dependent glutaminase response to liver injury and hyperbaric oxygenation.

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Activity of phosphate-dependent glutaminase was determined in hepatocytes of white female rats, both in healthy animals and in rats with chronic CCl4-hepatitis on day 3 after liver resection and hyperbaric oxygenation. In healthy animals, activity of phosphate-dependent glutaminase was not altered

[Correction of glutamine metabolism impairments in the operated liver with chronic hepatitis by hyperbaric oxygen].

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Application of hyperbaric oxygenation (HBO, 3 ata, 1 session for 50 min per day) during the first three days after liver resection (LR, 15-20% from the organ mass) in animals with chronic toxic hepatitis (CCl4, 50%, 0,1 ml/per 100 g of body mass, subcutaneously, once in 2 days, 65 days) eliminates a

[Glutamine metabolism in the liver after partial hepatectomy in chronic hepatitis].

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A long-term treatment of female rats with CCl4 caused a decrease of glutamine content in the liver. This decrease may be attributed to stable reduction of glutamine synthetase activity and slightly elevated (or unchanged) phosphate-dependent glutaminase. Partial hepatectony (15-20% of the liver) did

Structural and functional insights into Erwinia carotovora L-asparaginase.

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Bacterial L-asparaginases are enzymes that catalyze the hydrolysis of l-asparagine to aspartic acid. For the past 30 years, these enzymes have been used as therapeutic agents in the treatment of acute childhood lymphoblastic leukemia. Their intrinsic low-rate glutaminase activity, however, causes

Genetics in liver disease: new concepts.

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OBJECTIVE Recent advancements in genotyping technology have contributed to an accelerated dissemination of information on sequence variation associated with hepatobiliary diseases and/or quantitative traits. RESULTS Since the first genome-wide association study (GWAS) on genetic gallstone risk in

Cloning, expression, purification and characterisation of Erwinia carotovora L-asparaginase in Escherichia coli.

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BACKGROUND For the past 30 years, bacterial L-asparaginases have been used as therapeutic agents in the treatment of acute childhood lymphoblastic leukemia. It is found in a variety of organisms such as microbes, plants and mammals. Their intrinsic low-rate glutaminase activity, however, causes

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