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http://purl.uniprot.org/citations/15288813http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15288813http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15288813http://www.w3.org/2000/01/rdf-schema#comment"Brain acyl-CoA hydrolase (BACH) is responsible for most of the long-chain acyl-CoA hydrolyzing activity in the brain and is localized exclusively in neurons. There are two BACH isoforms: the major isoform, a 43-kDa BACH, and a lesser isoform, a 50-kDa BACH. In our previous work [Brain Res. Mol. Brain Res. 98 (2002) 81], a possibility was raised that these BACH isoforms might be generated from a single mRNA species via a mechanism of alternative use of translation start sites. However, the results obtained in the current study indicated that the 43-kDa BACH and 50-kDa BACH are not generated from a single mRNA species, but from distinct mRNA species transcribed by alternative use of transcription start sites. The molecular properties of the 50-kDa BACH were compared to those of the 43-kDa BACH. Palmitoyl-CoA hydrolase activity and protein stability were almost the same between both BACH isoforms. In addition, both 43-kDa BACH and 50-kDa BACH that were fused to green fluorescent protein showed cytosolic distribution. These results suggest that the 50-kDa BACH plays a similar role as the 43-kDa BACH. Therefore, since the 43-kDa BACH is expressed at higher levels than 50-kDa BACH, the 43-kDa BACH should largely contribute to understanding the physiological functions of the BACH gene in neurons."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2004.06.005"xsd:string
http://purl.uniprot.org/citations/15288813http://purl.org/dc/terms/identifier"doi:10.1016/j.abb.2004.06.005"xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/author"Takagi M."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/author"Takagi M."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/author"Suga T."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/author"Suga T."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/author"Yamada J."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/author"Yamada J."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/author"Kawabe K."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/author"Kawabe K."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/pages"100-105"xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/pages"100-105"xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/title"A 50-kDa isoform of mouse brain acyl-CoA hydrolase: expression and molecular properties."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/title"A 50-kDa isoform of mouse brain acyl-CoA hydrolase: expression and molecular properties."xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/volume"429"xsd:string
http://purl.uniprot.org/citations/15288813http://purl.uniprot.org/core/volume"429"xsd:string
http://purl.uniprot.org/citations/15288813http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15288813
http://purl.uniprot.org/citations/15288813http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15288813