Wyniki wyszukiwania - Biblioteka Nauki

1

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

100%

Suematsu N. , Okamoto K. , Isohashi F.

Acta Biochimica Polonica

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2002

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tom 49

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nr 4

937-945

EN

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.

2

Toxic effects of the crude methanolic extract of Austroplenckia populnea leaves and fractions on the growth of Spodoptera frugiperda

86%

Pires W. , Arini L. E. S. , Menezes A. C. S. , Jesus F. G. , Rocha E. C. , Araujo M. S.

Acta Agrobotanica

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2023

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tom 76

3

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

86%

Suematsu N. , Isohashi F.

Acta Biochimica Polonica

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2006

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tom 53

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nr 3

553-561

EN

A cDNA encoding human cytosolic acetyl-CoA hydrolase (CACH) was isolated from a human liver cDNA library, sequenced and functionally expressed in insect cells. The human CACH cDNA encodes a 555-amino-acid sequence that is 81.4%/78.7% identical to those of the mouse/rat homologue, suggesting a conserved role for this enzyme in the human and rodent livers. Bioinformatical study further reveals a high degree of similarity among the human and rodent CACHs as follows: First, the gene is composed of 15 exons ranging in size from 56 to 157 bp. Second, the protein consists of two thioesterase regions and a C-terminal steroidogenic acute regulatory protein-related lipid transfer (START) domain. Third, the promoter region is GC-rich and contains GC boxes, but lacks both TATA and CCAAT boxes, the typical criteria of housekeeping genes. A consensus peroxisome proliferator responsive element (PPRE) present in the rodent CACH promoter regions supports marked CACH induction in rat liver by peroxisome proliferator (PP).

4

Expression of viral genes in baculoviruses: immunogenicity of proteins

72%

Mizak B.

Bulletin of the Veterinary Institute in Puławy

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1998

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tom 42

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nr 1

5

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

58%

Suematsu N. , Okamoto K. , Isohashi F.

Acta Biochimica Polonica

|

2002

|

tom 49

|

nr 4

EN

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.

6

Beauvericin cytotoxicity to the invertebrate cell line SF-9

58%

Calo L. , Fornelli F. , Nenna S. , Tursi A. , Caiaffa M. F. , Macchia L.

Journal of Applied Genetics

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2003

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tom 44

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nr 4