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3 Acta Biochimica Polonica

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Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase

100%

Suematsu N. , Isohashi F.

Acta Biochimica Polonica

2006

tom 53

nr 3

Rapid and simple screening of transgenic mice: novel extraction-free, filter-based PCR genotyping from blood samples

100%

Suematsu N. , Isohashi F.

Acta Biochimica Polonica

2006

tom 53

nr 3

Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme involved in fat metabolisme: cDNA cloning sequencing and functional expression

80%

Suematsu N. , Okamoto K. , Isohashi F.

Acta Biochimica Polonica

2002

tom 49

nr 4

A cytosolic acetyl-CoA hydrolase (CACH) cDNA has been isolated from mouse liver cDNA library and sequenced. Recombinant expression of the cDNA in insect cells resulted in overproduction of active acetyl-CoA hydrolyzing enzyme protein. The mouse CACH cDNA encoded a 556-amino-acid sequence that was 93.5% identical to rat CACH, suggesting a conserved role for this enzyme in the mammalian liver. Database searching shows no homology to other known proteins, but reveals homological cDNA sequences showing two single-nucleotide polymorphisms (SNPs) in the CACH coding region. The discovery of mouse CACH cDNA is an important step towards genetic studies on the functional analysis of this enzyme by gene-knockout and transgenic approaches.