Search PubMed⌕ Search

Biomedical subjects

M Ogata

Publications and source records attributed to M Ogata.

At least 487 records · Page 27Linked to original sources
PubMed1983

Polyacrylamide gradient gel electrophoretic studies of residual catalase in acatalasemia.

Erythrocyte catalse in a Japanese-type acatalasemia and a normal control subject was separated by chromatofocusing with or without prior partial purification with DEAE-cellulose. Fractions were analyzed by polyacrylamide gradient gel electrophoresis for catalse activity and protein stain. Chromatofocusing revealed no marked difference in pI values between normal and acatalasemic catalases with or without partial purification. In the gel electrophoresis, molecular weights were also similar; two bands of catalase activity with molecular weights of 290,000 and 350,000 for the acatalasemia and of 280,000 and 360,000 for the normal control were found in the partially purified preparations. The molecular weight of normal catalase in untreated hemolysate was 250,000. Normal catalse was identified as protein bands on polyacrylamide gradient gel after fractionation of hemolysate by chromatofocusing. A more sensitive method for protein stain is still required for demonstration of residual catalse protein on the gel.

Acatalasia↗
PubMed1983

The oxidation mechanism of metallic mercury in vitro by catalase.

Magos et al reported the effect of 3-amino-1,2,4-triazole on mercury uptake by in vitro human blood samples and the mercury contents in blood and brain of rats exposed to metallic mercury vapor. The authors described the oxidation of metallic mercury by human blood cells having different catalase activities, hypocatalasemia and acatalasemia, with or without hydrogen peroxide. Kudsk found that ethyl alcohol inhibited the uptake of metallic mercury by blood in vitro and in vivo. These findings raise a question as to whether or not the inhibition by ethyl alcohol of the uptake of mercury by the blood is due to a direct reaction between ethyl alcohol and the catalase-hydrogen peroxide complex. The present report deals with the mechanism of metallic mercury oxidation in vitro by catalase using ethyl alcohol.

Animals↗
PubMed1983

Classification of potentially toxic chemicals based on their effects on mitochondrial respiration.

The classification of potentially toxic chemicals including environmental pollutants was made with respect to state 3 and state 4 respiration of mitochondria. The concentration of certain metals for 50% inhibition of respiratory control index (RCI; state 3/state 4) was lower than that of organic compounds tested. Various chemicals including environmental pollutants were classified into four groups by combination of effects on state 3 and state 4 respiration.

Animals↗
PubMed1982

Isolation of ureaplasmas from poultry and experimental infection in chickens.

Ureaplasmas were isolated from the oropharynxes of 47 of 247 (19 per cent) Leghorn chickens (Gallus gallus domesticus) and from five Japanese bantams but none was isolated from the oropharynx or cloaca of other poultry comprising 10 Japanese game, 75 common quails (Coturnix coturnix japonica), 17 turkeys (Meleagris gallopavo) and 10 guinea fowls (Numida galeata). In apparently healthy chickens, ureaplasmas were found at various sites, including the conjunctiva, nasal cavity, oropharynx, upper and lower tracheas, but not from the air sac, lungs, yolk, oviduct, urine or cloaca. All the isolates were antigenically similar but had no serological relation to those isolated from man, monkey, cattle, goat, sheep, dog and cat. In chickens experimentally infected with an avian ureaplasma, the organisms infected the oropharynx and nasal cavity but none of the birds inoculated demonstrated any clinical signs or macroscopic lesions.

Animals↗
PubMed1982

Mercury oxidation in vitro by ferric compounds.

Among the ferric compounds studied, cytochrome C, methemoglobin, lactoperoxidase, ferritin and ferric ion, in addition to catalase, had the ability to oxidize metallic mercury in the presence of hydrogen peroxide. On the other hand, hematin, the active center of catalase, did not oxidize metallic mercury. The results are consistent with the increased oxidation and uptake of mercury in the liver by acatalasemia mice.

Animals↗
PubMed1982

Distribution and accumulation of [2,3-14C]acrylonitrile in rat after single injection.

The distribution and accumulation of acrylonitrile after the single i.p. injection of [2,3-14C]acrylonitrile were examined by whole-body autoradiography and by the determination of 14C radioactivities in several tissues and subcellular fractions after a whole-body perfusion. 14C Radioactivity was seen strongly in blood, particularly in red blood cells, and in several tissues including lung, liver, and kidney. Longer retention of radioactivity in brain and muscle was observed. At the subcellular level a relatively high specific radioactivity was seen in cytosol fractions of the brain, liver, and kidney.

Acrylonitrile↗