acetyl-dl-carnitine hydrochloride
acetyl-dl-carnitine hydrochloride structure
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Common Name | acetyl-dl-carnitine hydrochloride | ||
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| CAS Number | 2504-11-2 | Molecular Weight | 239.69700 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C9H18ClNO4 | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | N/A | |
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In HepG2 cells, coexisting carnitine deficiency masks important indicators of marginal biotin deficiency.
J. Nutr. 145(1) , 32-40, (2015) A large number of birth defects are related to nutrient deficiencies; concern that biotin deficiency is teratogenic in humans is reasonable. Surprisingly, studies indicate that increased urinary 3-hydroxyisovalerylcarnitine (3HIAc), a previously validated mar... |
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Sodium-dependent carnitine transport in human placental choriocarcinoma cells.
Biochim. Biophys. Acta 1284 , 109-117, (1996) The JAR human placental choriocarcinoma cells were found to transport carnitine into the intracellular space by a Na(+)-dependent process. The transport showed no requirement for anions. The Na+-dependent process was saturable and the apparent Michaelis-Mente... |
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Photoaffinity labelling of carnitine acetyltransferase with S-(p-azidophenacyl)thiocarnitine.
Biochem. J. 237 , 533-540, (1986) A photolabile reagent, p-azidophenacyl-DL-thiocarnitine, was synthesized and tested as a photoaffinity label for carnitine acetyltransferase (EC 2.3.1.7) from pigeon breast. p-Azidophenacyl-DL-thiocarnitine is an active-site-directed reagent for this acetyltr... |
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Kinetic properties of purified carnitine acetyltransferase from the skeletal muscle of Arabian camel (Camelus dromedarius).
Biochimie 78 , 204-208, (1996) The kinetic properties of carnitine acetyltransferase from the skeletal muscle of the Arabian camel (Camelus dromedarius) were studied. The enzyme showed an optimum pH between 7.2 and 8.2. Reciprocal plots of data obtained by varying one substrate concentrati... |