Biography:

In the past Tamotsu Nakano has collaborated on articles with Tadayoshi Doke. One of their most recent publications is Mouse dopamine β-hydroxylase: primary structure deduced from the cDNA sequence and exon/intron organization of the gene. Which was published in journal Biochemical and Biophysical Research Communications.

More information about Tamotsu Nakano research including statistics on their citations can be found on their Copernicus Academic profile page.

Tamotsu Nakano's Articles: (3)

Mouse dopamine β-hydroxylase: primary structure deduced from the cDNA sequence and exon/intron organization of the gene

AbstractGenomic clones for mouse dopamine β-hydroxylase (DBH) were isolated from two genomic libraries derived from DBA/2J and 129/SV mouse strains, by plaque hybridization with the human DBH cDNA probe. Subsequently, cDNA encoding mouse DBH was amplified with reverse transcription-polymerase chain reaction (RT-PCR) method using primers corresponding to 5′- and 3′-portions of the mouse DBH mRNA, subcloned into a plasmid vector, and subjected to nucleotide sequence analysis. The clone encoded a protein of 621 amino acids with a calculated molecular mass of 70, 186 daltons. The predicted amino acid sequence of mouse DBH showed 87%, 80% and 79% identities with the rat, bovine and human enzymes, respectively. Several potential amino acid sequences that are involved in the posttranslational modification and catalytic function of DBH were identified in mouse DBH protein. Nucleotide sequence analysis of the overlapping genomic clones showed that the mouse DBH gene was composed of 12 exons about 17 kb in length. Typical TATAand CCAAT boxes were observed in the 5′-upstream region of the gene. Northern blot analysis of adrenal gland RNA detected a single size species of the mouse DBH mRNA.

Mouse dopamine β-hydroxylase: primary structure deduced from the cDNA sequence and exon/intron organization of the gene

AbstractGenomic clones for mouse dopamine β-hydroxylase (DBH) were isolated from two genomic libraries derived from DBA/2J and 129/SV mouse strains, by plaque hybridization with the human DBH cDNA probe. Subsequently, cDNA encoding mouse DBH was amplified with reverse transcription-polymerase chain reaction (RT-PCR) method using primers corresponding to 5′- and 3′-portions of the mouse DBH mRNA, subcloned into a plasmid vector, and subjected to nucleotide sequence analysis. The clone encoded a protein of 621 amino acids with a calculated molecular mass of 70, 186 daltons. The predicted amino acid sequence of mouse DBH showed 87%, 80% and 79% identities with the rat, bovine and human enzymes, respectively. Several potential amino acid sequences that are involved in the posttranslational modification and catalytic function of DBH were identified in mouse DBH protein. Nucleotide sequence analysis of the overlapping genomic clones showed that the mouse DBH gene was composed of 12 exons about 17 kb in length. Typical TATAand CCAAT boxes were observed in the 5′-upstream region of the gene. Northern blot analysis of adrenal gland RNA detected a single size species of the mouse DBH mRNA.

Dose equivalents inside the MIR Space Station measured by the combination of CR-39 plates and TLDs and their comparison with those on Space Shuttle STS-79, -84 and -91 missions

AbstractIn 1997, four dosimeter packages, each of which contains two CR-39 plates and 18 TLDs (Mg2SiO4:Tb), were placed inside the MIR Space Station and flew on an orbit with an inclination angle of 51.6° and an altitude of approximately 400km for 40 days. We estimated the absorbed doses, dose equivalents and effective quality factors during the flight by combining CR-39 data and TLD data. We then compared these results to those obtained with the same analysis method from the dosimeter packages on board Space Shuttle missions STS-79, -84 and -91 that flew along the same orbit. Finally, the differences between our results and those obtained by another group using passive dosimeters on the MIR are discussed.

Advertisement
Join Copernicus Academic and get access to over 12 million papers authored by 7+ million academics.
Join for free!

Contact us