beta glucuronidase/نخر

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[Measurement of serum immunoreactive beta-glucuronidase: a possible serological marker for histological hepatic cell necrosis and to predict the histological progression of hepatitis].

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beta-Glucuronidase, a lysosomal hydrolase, was purified from human liver tissue, and an enzyme-linked immunosorbent assay was developed using specific antibody against the enzyme. Using the assay procedure, the serum immunoreactive beta-glucuronidase (beta-glucuronidase) was determined in 190

Serum immunoreactive beta-glucuronidase determined by an enzyme-linked immunosorbent assay in patients with hepatic diseases.

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An enzyme-linked immunosorbent assay (ELISA) was developed for human beta-glucuronidase, using a specific polyclonal antibody raised against the purified enzyme. beta-Glucuronidase from human liver consisted of three subunits with molecular mass of 76, 64 and 18 kDa. The assay offered a specific,

Identification of an internal RNA element essential for replication and translational enhancement of tobacco necrosis virus A(C).

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Different regulatory elements function are involved in plant virus gene expression and replication by long-distance RNA-RNA interactions. A cap-independent functional element of the Barley yellow dwarf virus (BYDV) - like translational enhancer (BTE) is present in Tobacco necrosis virus A (TNV-A), a

Tumour necrosis factor beta (lymphotoxin) inhibits locomotion and stimulates the respiratory burst and degranulation of neutrophils.

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The data presented here demonstrate that recombinant human tumour necrosis factor beta (rHuTNF beta; lymphotoxin) is a neutrophil modulator. The lymphokine inhibited the locomotion of neutrophils and augmented the neutrophil oxygen-dependent respiratory burst in response to

Effects of tumour necrosis factor alpha and interleukin-1 alpha and beta on human neutrophil migration, respiratory burst and degranulation.

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Recombinant human tumour necrosis factor alpha (rHuTNF alpha) was shown to inhibit human neutrophil migration in the presence or absence of a chemotactic gradient generated with the tripeptide, N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMLP), at doses of 20-100 U/10(6) cells. In contrast,

Enhancement of lysosomal enzyme activity by recombinant human tumor necrosis factor and its role in tumor cell killing in vitro.

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We investigated the effect of recombinant human tumor necrosis factor (TNF) on the lysosomal enzyme activity of various established cell lines in vitro. Incubation of 1 x 10(6) TNF-sensitive mouse tumorigenic fibroblasts (L-M cells) in the presence of TNF (100 U/ml) for 48 h increased the total (the

Induction of β-glucuronidase release by cytostatic agents in small tumors.

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Extracellular β-glucuronidase (β-GUS) in tumors has been investigated as a target enzyme for prodrug therapy. However, despite encouraging preclinical results, animal studies also indicate that the success of prodrug therapy might be limited by the insufficient prodrug-converting enzyme activity,

Synergism between interleukin-8 and tumor necrosis factor-alpha for neutrophil-mediated platelet activation.

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We previously showed that two polymorphonuclear neutrophil (PMN)-derived proteinases, namely cathepsin G (Cat. G) and elastase (HLE), acting in synergy activated nearby platelets in vitro. This cellular interaction could result in a pathology such as the adult respiratory distress syndrome (ARDS).

Studies on intracardiac acid hydrolases in the ischemic myocardial necrosis.

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Activities and subcellular distributions of acid hydrolases, cathepsin D, acid phosphatase and beta-glucuronidase in myocardial subfractions were determined serially with reference to the initiation of myocardial necrosis in dog hearts with acute ischemia. The following results were obtained: 1) In

Acid hydrolases in the initiation of ischemic myocardial necrosis.

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Alterations in myocardial acid hydrolases in acute ischemia were studied in relation to the evolution of cardiac cellular necrosis by the determination of cathepsin D, acid phosphatase (AcPase), and beta-glucuronidase activities of the myocardial fractions and by electron microscopic cytochemical

Effects of interferon-gamma and tumor necrosis factor-alpha on macrophage enzyme levels.

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Murine peritoneal macrophages were treated with interferon-gamma (IFN-gamma) or tumor necrosis factor-alpha (TNF). Measurements of changes in acid phosphatase and beta-glucuronidase levels were made as an indication of activation by cytokine treatment. IFN-gamma or TNF-gamma treatment resulted in a

Chimeric TNT-3/human beta-glucuronidase fusion proteins for antibody-directed enzyme prodrug therapy (ADEPT).

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ADEPT (antibody-directed enzyme prodrug therapy) is a novel therapeutic approach that targets an enzyme into tumors to convert a relatively nontoxic prodrug into an active cytotoxic agent. This method has a number of advantages, including the reduction of systemic toxicity, but to date it has not

Expression of anti-tumor necrosis factor alpha (TNFα) single-chain variable fragment (scFv) in Spirodela punctata plants transformed with Agrobacterium tumefaciens.

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Therapeutic antibodies against tumor necrosis factor alpha (TNFα) have been considered effective for some of the autoimmune diseases such as rheumatoid arthritis, Crohn's diseases, and so on. But associated limitations of the current therapeutics in terms of cost, availability, and immunogenicity

Comparison of serum and urine fibrin split products and urinary beta-glucuronidase in the diagnosis of renal transplant rejection.

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This study compares the usefulness of serum and urine fibrin split products and the urinary enzyme, beta-glucuronidase, in the diagnosis and management of renal transplant rejection. Fibrin split products, determined by a tanned human red cell agglutination inhibition immunoassay, were measured as a

Association of lysosomal activity with sensitivity and resistance to tumor necrosis factor in murine L929 cells.

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The cytotoxic mechanism of action of tumor necrosis factor (TNF) was examined using murine L929 fibrosarcoma cells in vitro. Two cell lines were evaluated: parental TNF sensitive (L929S) (50% cytotoxic concentration, 2-6 ng/ml); and TNF resistant (L929R) (50% cytotoxic concentration, greater than

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