Results 181 to 190 of about 35,273 (228)
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Ornithine decarboxylase in perfused rat heart

Journal of Molecular and Cellular Cardiology, 1986
In the isolated perfused rat hearts, the activity of tissue ornithine decarboxylase gradually decreases over 90 min. In contrast, the activity of S-adenosylmethionine decarboxylase, lactate dehydrogenase, and glutamate-oxalacetate transaminase stays unchanged after a small decrease during the first 10 min.
S, Astancolle   +5 more
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Ornithine decarboxylase and S-adenosylmethionine decarboxylase in trypanosomatids

Biochemical Society Transactions, 2007
The production of polyamines has been shown to be an effective target for a drug against the West African form of sleeping sickness caused by Trypanosoma brucei gambiense. T. brucei belongs to the group of protozoan parasites classed as trypanosomatids.
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Ornithine decarboxylase activity in Entamoeba invadens

International Journal for Parasitology, 1993
Growth of E. invadens was paralleled by a concomitant increase in ornithine decarboxylase activity which peaked after 5 days of cultivation in TYI-S-33 medium. Over this period, enzyme activity increased about nine-fold with respect to that present at the start of incubation.
C, Calvo-Méndez   +2 more
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Sandwich Enzyme Immunoassay for Ornithine Decarboxylase

Journal of Immunoassay, 1989
A sensitive enzyme immunoassay (EIA) was developed for the determination of ornithine decarboxylase (ODC, EC 4.1.1.17), in the range of 0.02-10 ng, using an affinity-purified anti-ODC-Fab'-peroxidase conjugate. The amount of ODC protein was determined in crude extracts from the kidney of testosterone-treated mice, regenerating rat liver and human ...
M, Nishiyama   +4 more
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Allylisopropylacetamide induces rat hepatic ornithine decarboxylase

Journal of Biochemical Toxicology, 1987
AbstractIn rat liver, allylisopropylacetamide (AIA) treatment strongly induced (25‐fold) the activity of rat hepatic ornithine decarboxylase (ODC). By either the oral or the subcutaneous route, AIA produced a long‐lasting induction (30 to 40 hours) of hepatic ODC activity.
K T, Kitchin, J L, Brown
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Functional Regions of Ornithine Decarboxylase Antizyme

Biochemical and Biophysical Research Communications, 1994
Degradation of ornithine decarboxylase, a key enzyme in polyamine biosynthesis, is accelerated by the binding of antizyme, an ornithine decarboxylase inhibitory protein induced by polyamines. In the present study, we examined the effects of a series of deletion mutants of rat antizyme.
T, Ichiba   +6 more
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Hormonal stimulation of hepatic ornithine decarboxylase

Biochemical and Biophysical Research Communications, 1971
Abstract Hepatic ornithine decarboxylase activity in adrenalectomized rats was increased by a variety of hormones, including hydrocortisone, growth hormone, insulin, glucagon, and thyroxin. Repeated treatment with either hydrocortisone or growth hormone, the most effective of the hormones tested, failed to maintain the elevated enzyme levels attained
W B, Panko, F T, Kenney
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Ornithine decarboxylase inactivation in HeLa cells

Journal of Cellular Physiology, 1976
AbstractOrnithine decarboxylase (ODC) can be induced up to 100‐fold over basal levels four hours after addition of glutamine to the medium of HeLa cells growing in suspension culture. As demonstrated in several other cell types, ODC is inactivated very rapidly in HeLa cells, and the rate of inactivation is seen to vary with a half life of 9–15 minutes ...
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Ornithine Decarboxylase Antizyme in Mammalian Tissues

1988
Antizyme was first described by Canellakis and coworkers (1) as a protein inhibitor of ornithine decarboxylase which is induced in response to an elevated level of putrescine in cells in culture or in liver of rats treated with putrescine. It was characterized as protease-sensitive, nuclease- insensitive and heat-labile, while the inhibition is ...
M E, Brosnan, Y W, Hu
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Ornithine decarboxylase as target of chemotheraphy

Advances in Enzyme Regulation, 1985
Ornithine decarboxylase is a key enzyme in polyamine synthesis and growth of mammalian cells. In this chapter I review recent reports on the purification and properties of the pure enzyme, and on the localization, synthesis and regulation of the enzyme in the cell. The use of monospecific antibodies, radiolabeled irreversible inhibitors and cDNA clones
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