Results 161 to 170 of about 46,168 (209)
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Helicobacter pylori does not use spermidine synthase to produce spermidine
Biochemical and Biophysical Research Communications, 2017Helicobacter pylori is the primary pathogen associated to gastritis and gastric cancer. Growth of H. pylori depends on the availability of spermidine in vivo. Interestingly, the genome of H. pylori contains an incomplete set of genes for the classical pathway of spermidine biosynthesis.
Huawei Zhang, Shannon Wing Ngor Au
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Acetylation of spermidine in polyamine catabolism
Biochimica et Biophysica Acta (BBA) - General Subjects, 1980Treatment with thioacetamide (150 mg/kg) was used to enhance polyamine metabolism in rat liver. The increased uptake and catabolism of [14C]spermine and the changes of putrescine, spermidine and spermine concentrations indicated enhanced polyamine turnover rates.
N, Seiler, F N, Bolkenius, B, Knödgen
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Stabilization of 70S Ribosomes by Spermidine
Nature New Biology, 1971RIBOSOMAL subunits in Escherichia coli dissociate and reasso-ciate after each round of translation1, but it is not known whether separation occurs at termination of protein synthesis2, or whether they are released as “free” 70S ribosomes and subsequently dissociate3.
S J, Hardy, G, Turnock
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Putrescine and spermidine transport in Leishmania
Molecular and Biochemical Parasitology, 2000The transport of putrescine and spermidine into Leishmnania donovani promastigotes and Leishmania mexicana promastigotes and amastigotes has been characterised. Polyamine transport was shown to be saturable and temperature-sensitive for both developmental stages of Leishmania.
M, Basselin, G H, Coombs, M P, Barrett
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Enzymic assay for spermine and spermidine
Analytical Biochemistry, 1966Abstract This paper describes a sensitive enzymic micromethod for the quantitative assay of spermine and spermidine. The method is based on the oxidation of the polyamines by serum amine oxidase. The aminoaldehydes produced during the oxidation are assayed by N -methyl-2-benzothiazolone hydrazone hydrochloride, at 660 mμ.
U, Bachrach, B, Reches
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Spermidine: A constituent of the myelin sheath?
Neuroscience Letters, 1978Abstract Spermidine, an aliphatic polyamine present in high concentrations in the white matter, could act as a bivalent ligand stabilizing myelin lamellae. To seek an answer to the title's question, polyamines were extracted from the subcellular fractions of rat brain after intracerebral injection of [14C]putrescine, a precursor of spermidine ...
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Structure and Mechanism of Spermidine Synthases
Biochemistry, 2007Aminopropyltransferases transfer aminopropyl groups from decarboxylated S-adenosylmethionine to amine acceptors, forming polyamines. Structural and biochemical studies have been carried out with the human spermidine synthase, which is highly specific for putrescine as the amine acceptor, and the Thermotoga maritima spermidine synthase, which prefers ...
Hong, Wu +7 more
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A New Pathway for the Biosynthesis of Spermidine
Biochemical Society Transactions, 1976The only pathway known for the biosynthesis of sperrnidine is from putrescine and S-adenosylmethionine. S-Adenosylmethionine is decarboxylated, and the aminopropyl group of the product is transferred to putrescine to form spermidine. The enzymes of this pathway, S-adenosylmethionine decarboxylase (EC 4.1.1 S O ) and aminopropyltransferase (EC 2.5.1.16),
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