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ascites/phosphatase
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Chemical and immunological characterization of rat ascites hepatoma alkaline phosphatase: a comparison with the liver enzyme.
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Alkaline phosphatase was purified from plasma membrane of rat ascites hepatoma AH-130 cells by chromatographies on DEAE-cellulose and Affi-Gel Blue and preparative polyacrylamide gel electrophoresis. The yield of the purified enzyme, finally as the denatured subunits, was about three times better
The effect of cancer chemotherapy on lysosomal enzymic activities (acid phosphatase) of Ehrlich ascites carcinoma cells.
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The distribution of acid phosphatase in Ehrlich ascites carcinoma cells was studied by histochemical techniques in mice treated with antitumoral agents (Tio-Tepa, Cosmegen). The results proved the accuracy of the histoenzymatic demonstration of APh activity for the study of early changes induced in
Purification and characterization of butyrate-induced protein phosphatase involved in apoptosis of Ehrlich ascites tumor cells.
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Short chain fatty acids including butyrate exhibit wide variety of biological effects towards cell growth, morphology and gene expression. In this report, we study the mechanism by which butyrate (BuA) modulates the expression of protein phosphatase when treated to the cells. As a model system, we
REEVALUATION OF ASSAYS USED TO SHOW RNA INDUCTION OF GLUCOSE-6-PHOSPHATASE IN ASCITES CELLS.
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The standard The standard procedures Glucostat method and Fiske-Subbarowphosphorus determination-are inadequate for the assay of glucose-6-phosphatase activity in Ehrlich ascites cells. Therefore, RNA induction of this enzyme in ascites cells, even if it occurs, cannot be demonstrated by thefe
GLUCOSE-6-PHOSPHATASE: REEXAMINATION OF THE RNA-INDUCED ACTIVITY IN MOUSE ASCITES TUMOR CELLS.
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The glucostat method for the measurement of glucose released by glucose-6-phosphatase has been reexamined; it is accurate and sensitive enough to measure glucose-6-phosphatase activity in mouse ascites tumor cells. In seven different experiments, treatment with RNA from liver led to increases in
Gene expression of protein phosphatases in rat ascites hepatoma cell lines.
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Gene expression of protein phosphatases 1 alpha, 1 gamma 1, 2A alpha, and 2C alpha in 14 rat ascites hepatoma cell lines was studied by Northern blot hybridization. The expression of PP1 alpha and PP2C alpha was increased and decreased, respectively, in all of the ascites hepatoma (AH) cells
Influence of carbon chain length of dietary fat on intestinal alkaline phosphatase in chylous ascites.
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The long-term effects of chain length of dietary fat on intestinal lymphatic transport of alkaline phosphatase were investigated in two patients with chylous ascites due to leakage of intestinal lymph into the peritoneal cavity. Substitution of a medium-chain triglyceride diet for long-chain
Discriminant responses of the catalytic unit and glucose 6-phosphate transporter components of the hepatic glucose-6-phosphatase system in Ehrlich ascites-tumor-bearing mice.
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The effect of Ehrlich ascites tumor cells, in vivo, on the hepatic glucose-6-phosphatase (G6Pase) system was examined. The V(max) for glucose 6-phosphate hydrolysis by G6Pase was reduced by 40% and a greater than 15-fold decrease in mRNA encoding the catalytic unit of the G6Pase system was observed
Selective high expression of protein phosphatase pp1-alpha messenger-RNA in rat poorly differentiated ascites hepatomas.
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We have examined the mRNA levels for the catalytic subunits of three phosphoseryl/phosphothreonyl protein phosphatases PP1alpha, PP2Aalpha and PP2C by Northern blot analysis in the three primary hepatomas and the three poorly differentiated ascites hepatomas. The mRNA levels were compared with those
Neoplastic alterations in subcellular distribution of type 1 alpha protein phosphatase in rat ascites hepatoma cells.
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Neoplastic alterations of type 1 alpha protein phosphatase (PP1 alpha) have been studied in rat ascites hepatoma cells, using regenerating liver after partial hepatectomy and normal rat liver as controls. In the particulate fraction of hepatomas, potential PP1 activity and the amount of PP1 alpha
An altered T2 beta translocase of the glucose-6-phosphatase system in the membrane of the endoplasmic reticulum from livers of Ehrlich-ascites-tumour-bearing mice.
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The inhibitory interactions of orthophosphate (P1) with the glucose-6-phosphatase system of intact microsomes derived from the livers of normal and Ehrlich-ascites-tumour-bearing mice reveal the appearance of a novel form of the T2 beta translocase component of the glucose-6-phosphatase system in
The hepatic glucose-6-phosphatase system in Ehrlich-ascites-tumour-bearing mice.
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To examine the effects of the presence of Ehrlich ascites tumours on both the catalytic unit and the substrate/product translocase components of the glucose-6-phosphatase system in vivo, we isolated microsomes from the livers of control and tumour-bearing mice. Samples were analysed immunochemically
Purification and characterization of alkaline phosphatase from plasma membranes of rat ascites hepatoma.
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Alkaline phosphatase was purified from plasma membranes of rat ascites hepatoma AH-130, the homogenate of which had 50-fold higher specific activity than that found in the liver homogenate. The presence of Triton X-100, 0.5%, was essential to avoid its aggregation and to stabilize its activity. The
The activities of aminoacyl-tRNA synthetase phosphatase and aminoacyl-tRNA synthetases in MPC-11 and Krebs II ascites cells.
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The activity of aminoacyl-tRNA synthetase phosphatase as well as the activities of aminoacyl-tRNA synthetases in Krebs II ascites cells and MPC-11 cells have been investigated. The activity of the phosphatase was greater in the tumor cells than in normal tissues. The aminoacyl-tRNA synthetase
Contrast manifestation of alkaline phosphatase and 5'-nucleotidase in plasma membranes isolated from rat liver and ascites hepatoma.
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1. Plasma membranes were isolated from ascites hepatoma AH-130 and rat livers with or without partial hepatectomy or bile duct ligation. Reciprocal manifestations of two marker enzymes for plasma membranes were observed in these membrane preparations; alkaline phosphatase activity was found much
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