http://purl.uniprot.org/citations/2351134 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2351134 | http://www.w3.org/2000/01/rdf-schema#comment | "Carnitine acetyltransferase was purified from the supernatant obtained after centrifugation of human liver homogenate to a final specific activity of 78.75 unit.mg-1 with acetyl-CoA as a substrate. Human carnitine acetyltransferase is a monomer of 60.5 kDa with maximum activity in the presence of propionyl-CoA and a pH optimum of 8.7. Apparent Km values for acetyl-CoA are three times lower than for decanoyl-CoA. Km values for L-carnitine in the presence of acetyl-CoA are six times lower than in the presence of decanoyl-CoA. Km values for acetylcarnitine are three times lower than for octanoylcarnitine. The polyclonal antibodies against human carnitine acetyltransferase recognize a 60.5-kDa peptide in the purified preparation of human liver and brain homogenates and in immunoblots of mitochondrial and peroxisomal fractions from human liver. Immunoprecipitation and SDS/PAGE analysis of 35S-labelled proteins produced by human fibroblasts indicate that mitochondrial carnitine acetyltransferase is synthesized as a precursor of 65 kDa. We also purified carnitine acetyltransferase from the pellet obtained after centrifugation of liver homogenate. The pellet was extracted by sonication in the presence of 0.5% Tween 20. The chromatographic procedures for the purification and the kinetic, physical and immunological properties of pellet-extracted carnitine acetyltransferase are similar to those of carnitine acetyltransferase purified from the supernatant of human liver homogenate."xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1990.tb15520.x"xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/author | "Finocchiaro G."xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/author | "Garavaglia B."xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/author | "Didonato S."xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/author | "Colombo I."xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/author | "Giardini R."xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/author | "Bloisi W."xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/name | "Eur J Biochem"xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/pages | "539-546"xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/title | "Purification and properties of carnitine acetyltransferase from human liver."xsd:string |
http://purl.uniprot.org/citations/2351134 | http://purl.uniprot.org/core/volume | "189"xsd:string |
http://purl.uniprot.org/citations/2351134 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2351134 |
http://purl.uniprot.org/citations/2351134 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/2351134 |
http://purl.uniprot.org/uniprot/P43155#attribution-6A010664DCC2DAA1D11646E36B39C1C4 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/2351134 |
http://purl.uniprot.org/uniprot/#_P43155-mappedCitation-2351134 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/2351134 |
http://purl.uniprot.org/uniprot/P43155 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/2351134 |