@article{MTMT:1426933,
	title = {Isolation and characterization of carnitine acetyltransferase from S. cerevisiae.},
	url = {https://m2.mtmt.hu/api/publication/1426933},
	author = {Kispál, Gyula and Cseko, J and Alkonyi, István and Sándor, Attila},
	doi = {10.1016/0005-2760(91)90097-2},
	journal-iso = {BIOCHIM BIOPHYS ACTA},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA},
	volume = {1085},
	unique-id = {1426933},
	issn = {0006-3002},
	abstract = {Carnitine acetyltransferase was isolated from yeast Saccharomyces cerevisiae with an apparent molecular weight of 400,000. The enzyme contains identical subunits of 65,000 Da. The Km values of the isolated enzyme for acetyl-CoA and for carnitine were 17.7 microM and 180 microM, respectively. Carnitine acetyltransferase is an inducible enzyme, a 15-fold increase in the enzyme activity was found when the cells were grown on glycerol instead of glucose. Carnitine acetyltransferase, similarly to citrate synthase, has a double localization (approx. 80% of the enzyme is mitochondrial), while acetyl-CoA synthetase was found only in the cytosol. In the mitochondria carnitine acetyltransferase is located in the matrix space. The incorporation of 14C into CO2 and in lipids showed a similar ratio, 2.9 and 2.6, when the substrate was [1-14C]acetate and [1-14C]acetylcarnitine, respectively. Based on these results carnitine acetyltransferase can be considered as an enzyme necessary for acetate metabolism by transporting the activated acetyl group from the cytosol into the mitochondrial matrix.},
	keywords = {immunoblotting; Saccharomyces cerevisiae/*enzymology; Mitochondria/enzymology/metabolism; Carnitine O-Acetyltransferase/isolation & purification/*metabolism; Acetylcarnitine/metabolism},
	year = {1991},
	eissn = {1878-2434},
	pages = {217-222}
}

@article{MTMT:1060971,
	title = {Kinetic advantage of the interaction between the fatty acid β-oxidation enzymes and the complexes of the respiratory chain},
	url = {https://m2.mtmt.hu/api/publication/1060971},
	author = {Sümegi, Balázs and Porpáczy, Zoltán and Alkonyi, István},
	doi = {10.1016/0005-2760(91)90016-B},
	journal-iso = {BIOCHIM BIOPHYS ACTA},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA},
	volume = {1081},
	unique-id = {1060971},
	issn = {0006-3002},
	year = {1991},
	eissn = {1878-2434},
	pages = {121-128}
}

@article{MTMT:1426937,
	title = {Role of the liver in carnitine metabolism: the mechanism of development of carnitine-deficient status in guinea-pigs.},
	url = {https://m2.mtmt.hu/api/publication/1426937},
	author = {Alkonyi, István and Cseko, J and Sándor, Attila},
	journal-iso = {J CLIN CHEM CLIN BIOCHEM},
	journal = {JOURNAL OF CLINICAL CHEMISTRY AND CLINICAL BIOCHEMISTRY},
	volume = {28},
	unique-id = {1426937},
	issn = {0340-076X},
	abstract = {It was shown that carnitine deficiency and an impairment of the conversion of butyrobetaine into carnitine develops not only in ascorbic acid-deficient guinea-pigs but also in partially starved animals. We propose that the same mechanism, an absolute or relative ascorbic acid deficiency, is operating in both nutritional states. An increased urinary excretion greatly contributes to the development of carnitine deficiency in guinea-pigs, both in ascorbic acid deficiency and starvation. With respect to the greatly increased excretion, guinea-pig carnitine deficiency resembles the human disorder and may serve as model for it.},
	keywords = {Animals; Male; Guinea Pigs; Liver/*metabolism; Starvation/metabolism/urine; Carnitine/*deficiency/metabolism/urine; Betaine/analogs & derivatives/metabolism/urine; Ascorbic Acid Deficiency/*complications/metabolism/urine},
	year = {1990},
	pages = {319-321}
}

@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}
}

@article{MTMT:1426939,
	title = {Use of anion-exchange resin in F- form in sample processing for determination of carnitine.},
	url = {https://m2.mtmt.hu/api/publication/1426939},
	author = {Sándor, Attila and Cseko, J and Alkonyi, István},
	doi = {10.1016/0378-4347(89)80025-8},
	journal-iso = {J CHROMATOGR B},
	journal = {JOURNAL OF CHROMATOGRAPHY B},
	volume = {497},
	unique-id = {1426939},
	issn = {1570-0232},
	keywords = {Chromatography, High Pressure Liquid; radiometry; Chromatography, Ion Exchange; Carnitine/*metabolism/urine},
	year = {1989},
	eissn = {1873-376X},
	pages = {250-257}
}

@article{MTMT:1425640,
	title = {ENHANCED UPTAKE OF CARNITINE BY PERFUSED-RAT-LIVER FOLLOWING STARVATION},
	url = {https://m2.mtmt.hu/api/publication/1425640},
	author = {Kispál, Gyula and Melegh, Béla and Alkonyi, István and Sándor, Attila},
	doi = {10.1016/0005-2736(87)90360-9},
	journal-iso = {BIOCHIM BIOPHYS ACTA},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA},
	volume = {896},
	unique-id = {1425640},
	issn = {0006-3002},
	keywords = {Animals; Male; RATS; KINETICS; Rats, Inbred Strains; fasting; Perfusion; Liver/drug effects/*metabolism; Chlorides/pharmacology; Ouabain/pharmacology; Biological Transport/drug effects; Potassium Cyanide/pharmacology; Mersalyl/pharmacology; Lithium Chloride; Lithium/pharmacology; Dinitrophenols/pharmacology; 2,4-Dinitrophenol; Carnitine/*metabolism},
	year = {1987},
	eissn = {1878-2434},
	pages = {96-102}
}

@article{MTMT:1425634,
	title = {ESTER COMPOSITION OF CARNITINE IN THE PERFUSATE OF LIVER AND IN THE PLASMA OF DONOR RATS},
	url = {https://m2.mtmt.hu/api/publication/1425634},
	author = {Sándor, Attila and Kispál, Gyula and Melegh, Béla and Alkonyi, István},
	doi = {10.1111/j.1432-1033.1987.tb13719.x},
	journal-iso = {EUR J BIOCHEM},
	journal = {EUROPEAN JOURNAL OF BIOCHEMISTRY},
	volume = {170},
	unique-id = {1425634},
	issn = {0014-2956},
	keywords = {Animals; Male; RATS; ESTERS; Rats, Inbred Strains; Liver/*metabolism; fasting; Perfusion; Eating; Diabetes Mellitus, Experimental/metabolism; Carnitine/*analogs & derivatives/blood/*metabolism},
	year = {1987},
	eissn = {1432-1033},
	pages = {443-445}
}

@article{MTMT:1060978,
	title = {Interaction between NAD-dependent isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase complex, and NADH:ubiquinone oxidoreductase},
	url = {https://m2.mtmt.hu/api/publication/1060978},
	author = {Porpáczy, Zoltán and Sümegi, Balázs and Alkonyi, István},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {262},
	unique-id = {1060978},
	issn = {0021-9258},
	year = {1987},
	eissn = {1083-351X},
	pages = {9509-9514}
}

@article{MTMT:1060980,
	title = {ISOLATION AND CHARACTERIZATION OF 3-HYDROXYACYL COENZYME-A DEHYDROGENASE-BINDING PROTEIN FROM PIG-HEART INNER MITOCHONDRIAL-MEMBRANE},
	url = {https://m2.mtmt.hu/api/publication/1060980},
	author = {Kispál, Gyula and Sümegi, Balázs and Alkonyi, István},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {261},
	unique-id = {1060980},
	issn = {0021-9258},
	year = {1986},
	eissn = {1083-351X},
	pages = {14209-14213}
}

@article{MTMT:1425643,
	title = {RELEASE OF CARNITINE FROM THE PERFUSED RAT-LIVER},
	url = {https://m2.mtmt.hu/api/publication/1425643},
	author = {Sándor, Attila and Kispál, Gyula and Melegh, Béla and Alkonyi, István},
	doi = {10.1016/0005-2760(85)90033-5},
	journal-iso = {BIOCHIM BIOPHYS ACTA},
	journal = {BIOCHIMICA ET BIOPHYSICA ACTA},
	volume = {835},
	unique-id = {1425643},
	issn = {0006-3002},
	keywords = {Animals; Male; RATS; KINETICS; Rats, Inbred Strains; fasting; Biological Transport; Perfusion; Liver/drug effects/*metabolism; Potassium Cyanide/pharmacology; Dinitrophenols/pharmacology; 2,4-Dinitrophenol; Carnitine/*metabolism},
	year = {1985},
	eissn = {1878-2434},
	pages = {83-91}
}