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Ornithine decarboxylase properties

The use of suicide inhibitors of ornithine decarboxylase and arginine decarboxylase, coupled with the efficiency of incorporation of labelled precursors, led to the conclusion that arginine decarboxylase was the source of putrescine for tobacco alkaloids including 1 and 2 [46], Labelled spermidine was incorporated into 1 and 2, apparently via degradation to putrescine [47]. In vitro properties of the nicotine demethylase activity from Nicotiana otophora were characterized [59]. [Pg.183]

Assaraf, Y. G., Kahana, C., Spira, D. T. and Bachrach, U. (1988) Plasmodium falciparum Purification, properties, and immunochemical study of ornithine decarboxylase, the key enzyme in polyamine biosynthesis. Exp. Parasitol. 67 20-30. [Pg.128]

Caffeic Acid Phenethyl Ester (CAPE). CAPE, a phenolic compound with antioxidant properties, is an active ingredient derived from honeybee propolis (52). CAPE has antiviral, anti-inflammatory and antiproliferative properties. The compound differentially suppresses the growth of numerous human cancer cells and also inhibits tumor promoter-mediated processes in transformed cells (53,54). In transformed cells, CAPE induces apoptosis and inhibits the expression of the malignant phenotype (55,56). In addition, CAPE treatment attenuates the formation of azoxymethane-induced aberrant crypts and the activities of ornithine decarboxylase (ODC), tyrosin protein kinase, and lipoxygenase activity (57). Although the molecular basis for these multiple chemopreventive effects of CAPE is not clear, recent studies have demonstrated that CAPE is a potent and specific inhibitor of the transcription factor NF-kB (58). CAPE inhibited the activity and expression of COX-2 in the carrageenan air pouch model of inflammation as well as in TPA-treated human oral epithelial cells (59). CAPE was able to reduce neointimal formation by inhibiting NF-kB activation in a model of endothelial injury of rat carotid artery (60). [Pg.158]

Applebaum, D., Sabo, D.L., Fischer, E.H., and Morris, D.R. (1975) Biodegradative ornithine decarboxylase of Escherichia coli. Purification, properties, and pyridoxal 5 -phosphate binding site. Biochemistry, 14 (16), 3675-3681. [Pg.406]

The induction of arrested mammalian cells into the cell cycle has also been well characterized with respect to events that precede DNA synthesis itself. These include synthesis of RNA and the induction of synthesis of such enzymes as thymidine kinase and ornithine decarboxylase (see Baserga, 1976 Pardee et al., 1978, for reviews). Quiescent cells that have been infected by an adenovirus do not display the accumulation of RNA that is typical of serum-stimulated cells (Pochron et al., 1980), nor is synthesis of ornithine decarboxylase induced (Cheetham and Bellett, 1982). Both serum stimulation and adenovirus infection do induce synthesis of thymidine kinase (Kit et al., 1965 Takahashi et al., 1966 Ledinko, 1967 Zimmerman et al., 1970), but the effects of simultaneous treatment with a-methyl-or-nithine indicate that the pathways of induction are not the same this agent has little effect on induction of thymidine kinase by Ad5, but inhibits the response to serum (Cheetham and Bellett, 1982). It, therefore, seems fair to conclude from this brief survey of the properties of the process whereby adenoviruses induce cellular DNA synthesis... [Pg.318]

Enzymes present in the liver cytosol with short half-lives include ornithine decarboxylase, thymidine kinase, tyrosine aminotransferase, tryptophan oxygenase, hydroxymethylglutaryl-CoA reductase, serine dehydratase, and phosphoenolpyruvate carboxykinase. All of these enzymes have degradation rate constants greater than 0.1/h—more than 10 times more rapid than the average ka for liver cytosol proteins (Schimke, 1970). Perhaps a scrutiny of the group can provide information on the enzyme properties as well as the nature of reactions catalyzed by enzymes with rapid turnover rates. [Pg.234]

Most cultures from Collection IBSO produce lyases L-ornithine, L-arginine, and L-lysine decarboxylases. Neuraminidase (sialidase, or mucopolysaccharide - N-acetylneuraminilhydrolase) is the enzyme of the hydrolase group. As is usual neuraminidase activity is a property of pathogenic organisms. We found for the first time that luminous bacterial cultures of the species V. harveyi possess low neuraminidase activity. It may be probably one of the factors contributing to contamination of marine animals by luminous bacteria. [Pg.96]


See other pages where Ornithine decarboxylase properties is mentioned: [Pg.141]    [Pg.307]    [Pg.1021]    [Pg.262]    [Pg.369]    [Pg.60]    [Pg.239]    [Pg.517]    [Pg.482]    [Pg.93]    [Pg.188]    [Pg.122]    [Pg.143]    [Pg.14]    [Pg.285]    [Pg.287]   
See also in sourсe #XX -- [ Pg.291 , Pg.292 ]




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