Toshiro Inagaki

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Carbonic anhydrase II (CAII) was purified from erythrocytes of male Sprague-Dawley rats, and its localization in rat maxillary incisor epithelial cells at various stages of amelogenesis was studied by means of immunoperoxidase staining using a rat CAII-specific monoclonal antibody. In the most apical portion of the incisor, some CAII immunoreactivity was(More)
Electron microscopic examination of the effect of linoleic acid hydroperoxide on cultured smooth muscle cells from human umbilical artery revealed that incubation of the cells with 5.0 nmol/ml (in terms of malondialdehyde) of the hydroperoxide for 3 h caused a decrease in the electron density of the mitochondrial matrix and that dilatation of the(More)
In vitro synthesis of general acyl CoA dehydrogenase [EC 1.3.99.3], one of the mitochondrial flavoenzymes, was carried out to elucidate its biosynthetic mechanism. Poly(A)+ RNA isolated from pig kidney was translated in vitro using wheat germ lysate system and the synthesized enzyme was immunoprecipitated by the antibody against purified pig kidney general(More)
cDNA clone for general acyl CoA dehydrogenase (GAD) was isolated from a rat liver cDNA expression library in lambda gt11 using anti-pig kidney GAD antibody. Size of the isolated cDNA was estimated to be 1.5-1.6 kb. By immunological analysis of fusion protein and epitope selection, the cDNA clone was identified as that containing the GAD gene. Partial amino(More)
Using monoclonal antibody specific to rat carbonic anhydrase isozyme VI (CA VI), the isozyme was localized in the lacrimal gland. A minority of acini (less than 10% of the total) contained a few immunoreactive acinar cells. Enzyme histochemistry indicated that the CA VI-positive cells were the only cells possessing CA in the lacrimal acini. In the acinar(More)
Castration results in a rapid decrease in the activity of RNA polymerase I (or A) of isolated nuclei of rat prostates. The decrease was mainly ascribed to the diminution in the number of in vivo initiated RNA chains. The "free form" activity of the enzyme, however, which was estimated by the use of exogenous template and actinomycin D, increased 24 h after(More)
Different forms of rat liver medium-chain acyl CoA dehydrogenase (MCAD) (EC 1.3.99.3) were produced in Escherichia coli carrying expression plasmids (pRMCADm-1 approximately 9) differing at the 5'-region of the cDNA. The proteins expressed could be readily extracted from the cells. The protein (approximately 44 kDa) directed by pRMCADm-3 showed the highest(More)
Two cDNA clones for the alpha-subunit of rat liver electron transfer flavoprotein were isolated and their nucleotide sequences were determined. The longer cDNA contained a protein-coding region of 900 nucleotides and 3'-noncoding region of 335 nucleotides. The identity of the clone was confirmed by matching the amino acid sequence predicted from the cDNA(More)
Monoamine oxidase was purified from pig liver mitochondria to homogeneity. The enzyme sample contained a large amount of phospholipids. Depletion of lipids from the enzyme sample resulted in a decrease in its activity, while activity was restored by the binding of the lipid-depleted enzyme to phosphatidylcholine, phosphatidylethanolamine, or mitochondrial(More)
In vitro synthesis of D-amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminating), EC 1.4.3.3], one of the peroxisomal flavin enzymes, was performed using a rabbit reticulocyte lysate system in order to elucidate the biosynthetic pathway of the enzyme. The apparent molecular weight of the synthesized enzyme protein was the same as that of D-amino(More)
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