@article{MTMT:24658284,
	title = {Pharmacokinetics of L-carnitine},
	url = {https://m2.mtmt.hu/api/publication/24658284},
	author = {Evans, AM and Fornasini, G},
	doi = {10.2165/00003088-200342110-00002},
	journal-iso = {CLIN PHARMACOKINET},
	journal = {CLINICAL PHARMACOKINETICS},
	volume = {42},
	unique-id = {24658284},
	issn = {0312-5963},
	year = {2003},
	eissn = {1179-1926},
	pages = {941-967}
}

@article{MTMT:1426930,
	title = {Inhibition of carnitine biosynthesis by valproic acid in rats--the biochemical mechanism of inhibition},
	url = {https://m2.mtmt.hu/api/publication/1426930},
	author = {Farkas, Viktória and Bock-Marquette, Ildikó and Cseko, J and Sándor, Attila},
	doi = {10.1016/S0006-2952(96)00507-2},
	journal-iso = {BIOCHEMIC PHARMACOL},
	journal = {BIOCHEMICAL PHARMACOLOGY},
	volume = {52},
	unique-id = {1426930},
	issn = {0006-2952},
	abstract = {The anticonvulsive drug, valproic acid (VPA), inhibits the biosynthesis of carnitine, and may contribute in this way to carnitine deficiency associated with VPA therapy. The conversion of [3H]-butyrobetaine into [3H]-carnitine was determined 60 min following a single intraperitoneal (i.p.) dose of 1.2 mmol/kg VPA in rats. The fraction of radioactivity found in [3H]-carnitine in the liver decreased from 63.2 +/- 1.50% to 39.2 +/- 1.11% (mean +/- SEM). Total carnitine in the liver also decreased, whereas the precursor butyrobetaine increased from 5.01 +/- 0.71 nmol/g to 8.22 +/- 0.82 nmol/g (mean +/- SEM). VPA also exhibited a dramatic effect on the conversion of an unlabeled loading amount of butyrobetaine. The increment in total carnitine caused by butyrobetaine in liver was reduced from 161 +/- 15.4 nmol/g to 53.2 +/- 5.11 nmol/g (mean +/- SEM). These data prove that VPA reduces the flux through butyrobetaine hydroxylase (EC 1.14.11.1.). The drug in vitro, however, did not inhibit the enzyme directly. Searching for the mechanism of action, we found that VPA decreased the level of alpha-ketoglutarate (alpha-KG; a cofactor of butyrobetaine hydroxylase) from 73.5 +/- 2.90 nmol/g to 52.9 +/- 2.2 nmol/g (mean +/- SEM) in the liver. The level of 1-glutamate showed a rather dramatic decrease in the liver. Moreover, alpha-KG proved to have a protective role against VPA in the [3H]-butyrobetaine conversion experiment.},
	keywords = {Animals; Male; Humans; RATS; Liver/drug effects/metabolism; Rats, Wistar; Glutamic Acid/metabolism; Coenzyme A/metabolism; Acetyl Coenzyme A/metabolism; Valproic Acid/adverse effects/*pharmacology; Carnitine/*biosynthesis/deficiency; Anticonvulsants/adverse effects/*pharmacology; Ketoglutaric Acids/metabolism; Betaine/analogs & derivatives/metabolism},
	year = {1996},
	eissn = {1873-2968},
	pages = {1429-1433}
}

@article{MTMT:1060968,
	title = {Cloning and sequencing of a cDNA encoding Saccharomyces cerevisiae carnitine acetyltransferase. Use of the cDNA in gene disruption studies},
	url = {https://m2.mtmt.hu/api/publication/1060968},
	author = {Kispál, Gyula and Sümegi, Balázs and Dietmeier, K and Bock-Marquette, Ildikó and Gajdos, G and Tomcsányi, T and Sándor, Attila},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {268},
	unique-id = {1060968},
	issn = {0021-9258},
	keywords = {Molecular weight; Molecular Sequence Data; Base Sequence; amino acid sequence; immunoblotting; Sequence Analysis, DNA; Restriction Mapping; *Cloning, Molecular; Escherichia coli/genetics; Isoenzymes/genetics; Sequence Homology, Amino Acid; Mitochondria/enzymology; Magnetic Resonance Spectroscopy; Transformation, Bacterial; Saccharomyces cerevisiae/*enzymology/*genetics; DNA, Fungal/chemistry/genetics; DNA/chemistry/*genetics; Carnitine O-Acetyltransferase/chemistry/*genetics/metabolism},
	year = {1993},
	eissn = {1083-351X},
	pages = {1824-1829}
}

@article{MTMT:1426935,
	title = {Radioisotopic carnitine assay using Dowex 50 cation exchanger resin.},
	url = {https://m2.mtmt.hu/api/publication/1426935},
	author = {Sándor, Attila},
	journal-iso = {EUR J CLIN CHEM CLIN},
	journal = {EUROPEAN JOURNAL OF CLINICAL CHEMISTRY AND CLINICAL BIOCHEMISTRY},
	volume = {29},
	unique-id = {1426935},
	issn = {0939-4974},
	abstract = {At termination of the known radioisotopic carnitine assay the incubating mixture was applied to a column of Dowex 50 W x 8 (H+) resin. The [1-14C]acetyl-L-carnitine formed during the incubation bound to the resin, while the excess of [1-14C]acetyl-CoA was washed out with water. Then the radioactivity from the resin was eluted with NH4OH and water into counting vials. The assay is handy, takes much less (one-eights) resin than the known radioisotopic methods and the blank value is insensitive to sample volume.},
	keywords = {Humans; Carbon Radioisotopes/diagnostic use; Carnitine/*blood; *Cation Exchange Resins},
	year = {1991},
	pages = {347-349}
}

@article{MTMT:1426936,
	title = {Surplus acylcarnitines in the plasma of starved rats derive from the liver.},
	url = {https://m2.mtmt.hu/api/publication/1426936},
	author = {Sándor, Attila and Cseko, J and Kispál, Gyula and Alkonyi, István},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {265},
	unique-id = {1426936},
	issn = {0021-9258},
	abstract = {The method used here to assess the contribution of liver to plasma acylcarnitine is based on the idea that in rat, shortly after administration of [3H]butyrobetaine the [3H]carnitine appearing in the plasma derives from the liver and so does the acyl moiety of [acyl-3H] carnitine. In the perchloric acid extracts of plasma and liver, the ester fraction of total carnitine was determined by enzymatic analysis and that of [3H]carnitines was determined by high performance liquid chromatography. The ester fraction of total carnitine in the plasma of fed rats was 32.6% while that of [3H]carnitines was 67.9%, 1 h following injection of [3H]butyrobetaine. For 48 h starved rats the equivalent values were 54.2 and 84.0%, respectively. 24 h after the administration of [3H]butyrobetaine, the ester content became the same in the total and [3H]carnitines. That the newly synthesized carnitine was more acylated (67.9 versus 32.6%, fed) indicates that liver exports acyl groups with carnitine as carrier. The observation that the ester fraction in the newly synthesized plasma carnitine increased with fasting (84.0 versus 67.9%) indicates that the surplus plasma acylcarnitine in fasting ketosis derives from the liver. Perfused livers, however, released carnitine with the same ester content (60-61%) whether they were from fed or fasted animals. Probably, the increased plasma [acylcarnitine] in fasting develops not by an increased ester output from the liver but by an altered handling in extrahepatic tissues.},
	keywords = {Animals; Male; ACYLATION; RATS; Rats, Inbred Strains; Liver/*metabolism; Reference Values; Perfusion; Starvation/blood/*metabolism; Carnitine/*analogs & derivatives/blood/*metabolism; Betaine/analogs & derivatives/metabolism},
	year = {1990},
	eissn = {1083-351X},
	pages = {22313-22316}
}