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Biomedical subjects

T Taniguchi

Publications and source records attributed to T Taniguchi.

At least 937 records · Page 52Linked to original sources
PubMed1977

Pathological changes in chickens inoculated with reticuloendotheliosis-virus-contaminated Marek's disease vaccine.

A disease characterized by delayed growth, anemia, abnormal feathers, and leg paralysis occurred among chickens inoculated with Marek's disease vaccine over a period from spring to fall in 1974. These chickens were recognized among flocks inoculated with the vaccine produced by two vaccine makers. The affected ones were examined pathologically. Gross examination revealed a slight enlargement of peripheral nerves and atrophy of the spleen, thymus, and bursa of Fabricius. Histopathologically, the peripheral nerves had a mild cell infiltration of lymphoid and plasma cells, edema, degeneration of nerve fibers with Schwann's cell proliferation. Perivascular cuffings consisting mainly of lymphoid cells were seen in the brain and spinal cord. Atrophic changes displayed by prominent reduction of lymphocytes were recognized in the spleen, thymus, and bursa of Fabricius. Etiological examination suggested that most of the chickens examined might have been infected with reticuloendotheliosis virus and not with Marek's disease virus. The pathological changes observed in the peripheral nerves and central nervous system, however, were not distinguishable from those of Marek's disease.

Animals↗
PubMed1976

Studies on nitrotyrosine-82 and aminotyrosine-82 derivatives of adrenodoxin. Effects of chemical modification on the complex formation with adrenodoxin reductase.

The coordination structure of the iron-sulfur center of the nitrotyrosine and the aminotyrosine derivates of bovine adrenodoxin was investigated by electron paramagnetic resonance spectroscopy. The reduced form of both modified samples exhibited signals identical with those for the native protein at g= 1.94 and g=2.01. From these results together with optical absorption and chemical analyses, it was concluded that the coordination structure of the iron-sulfur chromophore for both the derivatives was identical with the binuclear tetrahedral structure of native adrenodoxin. The configuration of the iron-binding area in nitro- and amino-adrenodoxin was studied by ovserving the circular dichroism spectra between 350 and 600 nm. The maxima for the nitro or amino derivatives were all identical with those for the native protein but different in the magnitude of their molar ellipticity. The molar ellipticities at 440 nm were 45.8 X 10(3), 14.5 X 10(3), and 9.5 X 10(6) deg cm2 per mol of iron for native adrenodoxin, nitro or amino derivative, respectively. These results suggest that the chemical modification of the tyrosine residue causes a conformational change in the iron-binding area. We have previously reported that the enzymatic activities of these reconstituted nitro and amino derivatives toware cytochrome c reduction in the presence of adrenodoxin reductase and reduced nicotinamide adenine dinucleotide phosphate were 19 and 7% of native adrenodoxin, respectively. The cytochrome c reductase activities of nitro- and aminoadrenodixin were drastically affected by the ionic strength of the assay medium, as found in native adrenodoxin. Fluorometric titration of the reductase with aminoadrenodoxin revealed that aminoadrenodoxin forms a 1:1 molar complex with the reductase. These results suggest that both the nitro and amino derivatives form a complex with the reductase. The dissociation constants of nitro- and aminoadrenodoxin for the reductase were 6.1 X 10(-7)M and 3.3 X 10(-7) M at mu = 0.04 and 1.9 X 10(-6) M and 2.0 X 10(-6) M at mu = 0.20, respectively. Comparison of these values with those of native adrenodoxin (approximately 10(-9) M at mu = 0.04 and 2.2 X 10(-7) M at mu = 0.20) suggests that an increase in the dissociation constant for the reductase is responsible for the decreased electron transferring activity of the modified adrenodoxins.

Adrenodoxin↗
PubMed1976

Recrudescence of equine infectious anemia by treatment with immunosuppressive drugs.

Horses which had passed a few months to a few years asymptomatically after the last recurrence of equine infectious anemia (EIA) showed a typical febrile response after treatment with the immunosuppressive agent, dexamethasone (DM) or cyclophosphamide (CY). In horses showing a febrile response, EIA virus which had not been neutralized by neutralizing antibody previously produced was propagated. In DM-treated horses it disappeared from the blood soon after pyretolysis and antibody against the virus was produced promptly. In contrast, detectable viremia persisted in CY-treated horses for 10 to 84 days after pyretolysis. Antibody against the virus was barely produced for 42 to 126 days after treatment. After drug treatment, there was no decrease in neutralizing antibody previously produced. Then, it was inferred that this febrile response was due to propagation of an immunologically variant virus which might have been produced as a result of decline in cell-mediated immunity. The role of cellular mechanisms in the development of immunity to EIA was also discussed.

Animals↗
PubMed1976

Inoculation experiment of Marek's disease vaccine contaminated with a reticuloendotheliosis virus.

Two-day-old chicks were inoculated with one or ten doses of Marek's disease (MD) vaccine originated from the herpesvirus of turkeys (HVT) and contaminated with a reticuloendotheliosis virus (REV). As a result, they presented such symptoms as abnormality in the vane of remiges, undergrowth, anemia, and leg paralysis. These symptoms were the same as those induced by the same vaccine among chicks in the field. Control chicks which had been placed in the same house as those inoculated with the vaccine exhibited no abnormal signs. A persistent infection with REV was noticed in the vaccine-inoculated group. A horizontal infection with REV was the highest in the control group, which was followed by the group inoculated with one dose and that inoculated with ten doses in the order listed. The antibody response of chicks to HVT and MD virus was also inhibited by REV.

Animals↗
PubMed1976

Isolation of a reticuloendotheliosis virus from chickens inoculated with Marek's disease vaccine.

Over a period from spring to fall in 1974, a disease with delayed growth, anemia, abnormal feathers, and leg paralysis as main symptoms broke out in flocks of chickens inoculated with Marek's disease vaccine. A virus was isolated from affected birds in the field and the same lot of Marek's disease vaccine as inoculated into these birds. It had a common antigenicity to the T strain of reticuloendotheliosis virus (REV) and could not be discriminated from this strain on the basis of morphology or property. When chicks were inoculated with it, they presented essentially the same symptoms as the birds affected in the field. Since the disease was reproduced in this manner, it was presumed to have been caused by REV contained in the vaccine as contaminant. The virus persisted in the body for long time and also induced horizontal infection.

Animals↗
PubMed1975

Studies on NO2-Tyr82and NH2-Tyr82 derivatives of adrenodoxin. Effects of chemical modification on electron transferring activity.

Bovine apoadrenodoxin was treated with tetranitromethane to introduce a nitro group into the tyrosyl residue at position 82 of this protein. The degrees of nitration under the best conditions were estimated to be 90% and nearly 100% on the basis of amino acid analysis and the spectrophotometric method, respectively. An amino derivative was prepared by reducing the nitro group with sodium dithionite. The apoadrenodoxin derivatives could be reconstituted to have an iron-sulfur chromophore similar to the native adrenodoxin which contains a 1:1 molar ratio of labile sulfur to iron content and displays absorption peaks at 414 and 450 nm. The enzymatic acitivies of these reconstituted nitro and amino derivatives toward cytochrome c reduction in the presence of adrenodoxin reductase and NADPH were 19 and 7% of native adrenodoxin, respectively. We studied the kinetics of the direct reduction of the reconstituted amino derivative in the presence of NADPH and adrenodoxin reductase under anaerobic conditons. The initial rate of reduction for the amino derivative was 7% of the native adrenodoxin, which is in good agreement with its activity toward cytochrome c reduction. From these results, it is concluded that by modifying the tyrosyl residue at position 82 of the adrenodoxin polypeptide, the electron-transferring activity of the molecule is largely diminished.

Adrenodoxin↗
PubMed1975

Thermally induced conformational changes of tobacco mosaic virus and their protein assemblies.

The measurement of the fluorescence intensity of tryptophan residues showed that a reversible transition in the local structure took place between 20 degrees C and 30c in intact virus particles and reconstituted protein assemblies of the ordinary strain and the tomato strain of tobacco mosaic virus. During this transition the overall polymer structure was maintained. In the case of the bean strain of tobacco mosaic virus, however, the fluorescence intensity did not show any transition in the same temperature range. Such a difference between different strains gave some information on the location of tryptophan residues possibly involved in the local structure change. The fluorescence polarization of intact virus particles showed no change in the whole temperature range, but the polarization of the reconstituted protein assembly of the ordinary strain showed a transition at the same temperature as the fluorescence intensity. This suggested a difference in the freedom of the local structure between intact virus particles and reconstituted protein assemblies. Oligomers of these virus proteins were stable up to 45c and above this temperature, began to make an irreversible transition where the secondary structure of the monomer was partially broken but the oligomer structure was retained.

Circular Dichroism↗