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http://purl.uniprot.org/citations/10578051http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10578051http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10578051http://www.w3.org/2000/01/rdf-schema#comment"An acyl-CoA hydrolase, referred to as hBACH, was purified from human brain cytosol. The enzyme had a molecular mass of 100 kDa and 43-kDa subunits, and was highly active with long-chain acyl-CoAs, e.g. a maximal velocity of 295 micromol/min/mg and K(m) of 6.4 microM for palmitoyl-CoA. Acyl-CoAs with carbon chain lengths of C(8-18) were also good substrates. In human brain cytosol, 85% of palmitoyl-CoA hydrolase activity was titrated by an anti-BACH antibody, which accounted for over 75% of the enzyme activity found in the brain tissue. The cDNA isolated for hBACH, when expressed in Escherichia coli, directed the expression of palmitoyl-CoA hydrolase activity and a 44-kDa protein immunoreactive to the anti-BACH antibody, which in turn neutralized the hydrolase activity. The hBACH cDNA encoded a 338-amino acid sequence which was 95% identical to that of a rat homolog. The hBACH gene spanned about 130 kb and comprised 9 exons, and was mapped to 1p36.2 on the cytogenetic ideogram. These findings indicate that the long-chain acyl-CoA hydrolase present in the brain is well conserved between man and the rat, suggesting a conserved role for this enzyme in the mammalian brain, and enabling genetic studies on the functional analysis of acyl-CoA hydrolase."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a022544"xsd:string
http://purl.uniprot.org/citations/10578051http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a022544"xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Endo T."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Endo T."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Hirata M."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Hirata M."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Watanabe T."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Watanabe T."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Taniguchi T."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Taniguchi T."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Kurata A."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Kurata A."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Furihata T."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Furihata T."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Suga T."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Suga T."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Yamada J."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Yamada J."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Takama H."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Takama H."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Iida N."xsd:string
http://purl.uniprot.org/citations/10578051http://purl.uniprot.org/core/author"Iida N."xsd:string