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Ascites cells

Horikawa and Fox (1964) isolated single cells from Drosophila embryos and were able to propagate these with the diploid chromosome number for years. [Pg.114]

Several cell lines have been isolated (Echalier and Ohanessian, [Pg.114]

Cell lines of Aedes aegypti (Grace, 1966) and A. albopictus (Singh, 1967) have been isolated as follows  [Pg.114]

In this medium cells of A. albopictus will double every 10-11 h and have the following cell cycle phase times calculated using the graphical analysis method (Fig 10.12). [Pg.114]

These figures are quite similar to those found in vivo for brain cells of A. Aegypti (Marchi and Rae, 1978). [Pg.115]


L Na -iiidepeiideiit Braiiched-chaiii and aromatic amino acids Ehrlich ascites cells Chinese hamster ovary cells Hepatocytes... [Pg.311]

Hall IH, Liou YF, Lee KH. Antitumor agents LII The effects of molephantinin on nucleic acid and protein synthesis of Ehrlich ascites cells. J Pharm Sci 1982 71 687-690. [Pg.230]

Hamza, M., Lloveras,J., Ribbes, G., Soula, G. and Douste-Blazy, L. (1983) An in vitro study of hemicholinium-3 on phospholipid metabolism of Krebs II ascites cells. Biochemical Pharmacology 32, 1893—1897. [Pg.419]

The application of forward chemical genetics to studies of translation provides an opportunity to identify small molecules that inhibit or stimulate this process without any underlying assumptions as to which step is most amenable to targeting by the chemical libraries under consideration. The opportunity exists to identify novel factors involved in translation, unravel new activities of known translation initiation factors, or characterize shortlived intermediates that are frozen by the small molecule inhibitor. We have undertaken a forward chemical genetic approach to identify small molecules that inhibit or stimulate translation in extracts prepared from Krebs-2 ascites cells (Novae et al., 2004). These screens have led to the identification of several novel inhibitors of translation initiation and elongation (Bordeleau et al., 2005, 2006 Robert et al., 2006a,b). [Pg.315]

Grassetti, D.R., and Murray, J.F. (December 1967) The effect of 2,2 -dithiodipyridine on thiols and oxi-dizable substrates of Ehrlich ascites cells and of normal mouse tissues. Biochem. Pharmacol. 16(12), 2387-2393. [Pg.1068]

Olson MO, Ezrailson EG, Guetzow K, Busch H (1975) Localization and phosphorylation of nuclear, nucleolar and extranucleolar non-histone proteins of Novikoff hepatoma ascites cells. J Mol Biol 97 611-619... [Pg.142]

Orphanides G, LeRoy G, Chang CH, Luse DS, Reinberg D (1998) FACT, a factor that facilitates transcript elongation through nucleosomes. Cell 92 105-116 Orrick LR, Olson MO, Busch H (1973) Comparison of nucleolar proteins of normal rat Uver and Novikoff hepatoma ascites cells by two-dimensional polyacrylamide gel electrophoresis. Proc Natl Acad Sci USA 70 1316-1320... [Pg.142]

D. Garfinkel and B. Hess, Metabolic control mechanisms. VII. A detailed computer model of the glycolytic pathway in ascites cells. J. Biol. Chem. 239, 971-983 (1964). [Pg.287]

Chromatographic evidence has been obtained for the formation of 6-thioguanosine di- and triphosphates in Ehrlich ascites cells [197] and their formation is supported by the demonstrated incorporation of thioguanine into nucleic acids as thioguanylic acid [198]. The incorporation of both the a- and 3-anomers of 2 -deoxythioguanosine (XXXVI) [199] into DNA without... [Pg.82]

Cordycepin-1-oxide (XLVIIl) is activated in Ehrlich ascites cells by reduction to cordycepin [220] and a similar A -oxide reduction probably underlies the action of 6-mercaptopurine-3-oxide (XLIX) [221]. [Pg.85]

The effect of 6-mercaptopurine on the incorporation of a number of C-labelled compounds into soluble purine nucleotides and into RNA and DNA has been studied in leukemia L1210, Ehrlich ascites carcinoma, and solid sarcoma 180. At a level of 6-mercaptopurine that markedly inhibited the incorporation of formate and glycine, the utilization of adenine or 2-aminoadenine was not affected. There was no inhibition of the incorporation of 5(or 4)-aminoimidazole-4(5)-carboxamide (AIC) into adenine derivatives and no marked or consistent inhibition of its incorporation into guanine derivatives. The conversion of AIC to purines in ascites cells was not inhibited at levels of 6-mercaptopurine 8-20 times those that produced 50 per cent or greater inhibition of de novo synthesis [292]. Furthermore, AIC reverses the inhibition of growth of S180 cells (AH/5) in culture by 6-mercaptopurine [293]. These results suggest that in all these systems, in vitro and in vivo, the principal site at which 6-mercaptopurine inhibits nucleic acid biosynthesis is prior to the formation of AIC, and that the interconversion of purine ribonucleotides (see below) is not the primary site of action [292]. Presumably, this early step is the conversion of PRPP to 5-phosphoribosylamine inhibited allosterically by 6-mercaptopurine ribonucleotide (feedback inhibition is not observed in cells that cannot convert 6-mercaptopurine to its ribonucleotide [244]. [Pg.94]

The significance of these in vitro enzyme inhibition studies is uncertain, in view of the evidence that has been presented concerning the sensitivity of cancer cells to feedback inhibition by these nucleotides. On the other hand, 6-chloropurine inhibits the de novo biosynthesis of nucleic acid guanine but not of nucleic acid adenine in sarcoma 180 ascites cells [319],... [Pg.98]

D-Arabinofuranosyladenine, presumably as the triphosphate, inhibits the incorporation of precursors into DNA [154], and the triphosphate inhibits non-competitively the incorporation of thymidine triphosphate into DNA in extracts of ascites cells, suggesting a direct interaction with DNA polymerase, possibly at an allosteric site [155]. Other studies have confirmed the inhibition of DNA synthesis catalyzed by DNA polymerase [335, 335a]. [Pg.99]

Fig. 2 a) Results of gel fraction assay on cytoplasmic extracts of Ehrlich ascites cells (after Ishiura and 0kada(13)). [Pg.229]

Hall, I. H., . H. Lee, W. L. Williams, T. Kimura, and T. Hiryama. 1980. Antitumor agents XLI effects of eupaformosanin on nucleic acid, protein, and anerobic and aerobic glycolytic metabolism of Ehrlich ascites cells. J. Pharm. Sci. 69 294-297. [Pg.335]

A cyanide-sensitive NAD(P)H dependent superoxide generating system was described, however, for the nuclear membrane of hepatoma 22 a ascites cells grown in mice... [Pg.5]

In some cases with crude preparations from higher plants, it has been shown that the cell volume increased highly, and neoplasmic cell vacuolization was observed. As a result of the administration of polysaccharides, the membranes of Ascites cells showed increased permeability to solutes and, consequently, the cell inhibed more water and swelled. [Pg.29]

Inhibition of mainly DNA synthesis has been shown for Ehrlich ascites cells (43) and human HV3 cells (43a), as studied by the uptake of radiolabeled DNA, RNA, and protein precursors. However, RNA and protein inhibition are still being examined (44). [Pg.181]

The nine steps involved in the purification of UMP synthase from starting tissue are outlined in figure 6.8. All steps were carried out at 0-5°C. About 200 g of Ehrlich ascites cells, a mammalian tumor rich in the desired enzymes, was suspended in buffer and processed in a tissue homogenizer, which mechanically breaks down the tissue... [Pg.125]

Epistephanine Weakly active in vitro against HeLa cells not active in vivo (mouse) against Ehrlich ascites cells 360... [Pg.146]

Fangchinoline Active against HeLa cells in vitro, not active toward Ehrlich ascites cells in mouse 360... [Pg.146]

Active against HeLa-S3 cells in vitro ineffective in vivo toward Ehrlich ascites cells in mice 360... [Pg.148]

Ineffective in inhibiting mitochondrial respiration of Ehrlich ascites cell suspensions 458... [Pg.149]

Thalicberine Active against HeLa and Ehrlich ascites cells in 360... [Pg.153]

Colombini, M. Johnstone, R.M. (1974). Na+ gradient stimulated AIB transport in membrane vesicles from Ehrlich ascites cells. J. Membr. Biol. 18, 315-334. [Pg.115]

McCormick, J.I. Johnstone, R.M. (1988a). Simple and effective purification of a Na+-dependent amino acid transport system from Ehrlich ascites cell plasma membrane. Proc. Natl. Acad. Sri. USA 85,7877-7881. [Pg.119]


See other pages where Ascites cells is mentioned: [Pg.123]    [Pg.202]    [Pg.238]    [Pg.76]    [Pg.80]    [Pg.86]    [Pg.450]    [Pg.8]    [Pg.274]    [Pg.275]    [Pg.277]    [Pg.296]    [Pg.55]    [Pg.127]    [Pg.205]    [Pg.32]    [Pg.105]    [Pg.109]   


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Ascites

Ascites sarcoma-7 cells

Ascites tumor cells

Ascites tumour cells

Cells ascites hepatoma

Ehrlich ascites cells

Ehrlich ascites tumor cells

Ehrlich-Ascites carcinoma cells

Ehrlich-Ascites tumour cells

Krebs II ascites cells

Mechanism ascites cells

Mouse ascites cells

Tumor cells, Erlich-Ascites

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