PubMed Health⌕ Search

Biomedical subjects

T Yamanaka

Publications and source records attributed to T Yamanaka.

At least 19 recordsLinked to original sources
PubMed1979

Paralytic poliomyelitis in a child with agammaglobulinemia.

This paper gives the clinical, immunological and virological data on a patient with agammaglobulinemia who developed paralytic poliomyelitis. The patient was a 3 year-old boy who had a typical B-cell defect without a T-cell defect. He had profound hypogammaglobulinemia and defective plasma cells and had repeated pyogenic infections which were controlled by gammaglobulin replacement therapy. At 3 years of age, he was admitted to our hospital with suspected meningitis. He had fewer, tremor and neck stiffness for 3 days and subsequently developed paralysis in his left arm and right leg. There was lymphocytosis in the cerebrospinal fluid. A non vaccine-like strain of poliovirus type 2 was isolated from the stool.

Agammaglobulinemia↗
PubMed1979

Flavocytochrome c of Chromatium vinosum. Some enzymatic properties and subunit structure.

The function and the structural features of Chromatium vinosum cytochrome c-552 have been investigated. Cytochrome c-552 has a sulfide-cytochrome c reductase activity and also catalyzes the reduction of elementary sulfur to sulfide with reduced benzylviologen as the electron donor. In the sulfide-cytochrome reduction, horse and yeast cytochromes c act as good electron acceptors, but cytochrome c' or cytochrome c-553(550) purified from the organism does not. The subunit structure of cytochrome c-552 has been studied. The cytochrome is split by 6 M urea into cytochrome and flavoprotein moieties with molecular weights of 21,000 and 46,000, respectively. The flavoprotein moiety is obtained by isoelectric focusing in the presence of 6 M urea and 0.1% beta-mercaptoethanol, while the hemoprotein moiety is obtained by gel filtration with Sephacryl S-200 in the presence of 6 M urea and 0.1 M KCl. Neither subunit has sulfide-cytochrome c reductase activity. Attempts to reconstitute the original flavocytochrome c from the subunits have been unsuccessful.

Amino Acids↗
PubMed1979

Subunits of cytochrome a-type terminal oxidases derived from Thiobacillus novellus and Nitrobacter agilis.

Cytochrome a-type terminal oxidases derived from Thiobacillus novellus and Nitrobacter agilis have been purified to a homogeneous state as judged from their electrophoretic behavior and their subunit structures studied by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The T. novellus enzyme is composed of two kinds of subunits of 32,000 and 23,000 daltons and its minimum molecular weight is 55,000 on the basis of heme content and amino acid composition. The N. agilis enzyme also has two kinds of subunits of 40,000 and 27,000 daltons and its minimum molecular weight is 66,000 on the basis of heme content and amino acid composition. Therefore, the molecule of each enzyme is composed of two kinds of subunits which resemble the subunits of the eukaryotic cytochrome oxidase biosynthesized in the mitochondrion at least with respect to molecular weight.

Electron Transport Complex IV↗
PubMed1979

Highly purified hydroxylamine oxidoreductase derived from Nitrosomonas europaea. Some physicochemical and enzymatic properties.

Hydroxylamine oxidoreductase [EC 1.7.3.4] of Nitrosomonas europaea was purified to an electrophoretically homogeneous state and some of its properties were studied. The molecular weight of the enzyme as determined by gel filtration on Sephadex G150 and by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate is 175,000-180,000, while the minimum molecular weight per heme determined from the dry weight and heme content is 17,500. The enzyme is a C-type cytochrome; its reduced form shows absorption peaks at 418 (gamma peak), 521 (beta peak), 553 (alpha peak), and 460 nm (due to an unidentified chromophore). Although the alpha peak at 553 nm has a shoulder at 559 nm, the enzyme does not posses protoheme or a cytochrome b subunit. It seems likely that the enzyme molecule possess heme c molecules in different states. The enzyme reacts rapidly with various eukaryotic cytochromes c, but does not react with "bacterial-type" cytochromes c. Although the enzyme does not react with cytochrome c-552 (N. europaea), another C-type cytochrome of the organism, cytochrome c-554 (N. europaea) acts as an electron acceptor for the enzyme.

Cyanides↗
PubMed1978

The alpha2-plasmin inhibitor levels in liver diseases.

Concentrations of alpha-2 plasmin inhibitor, which is a primary and fast-reacting inhibitor of plasmin, were measured immunochemically in sera of patients with liver diseases and compared with normal controls. Serum level of alpha2-plasmin inhibitor was significantly decreased in liver cirrhosis and other severely affected liver diseases. The decrease appeared to be dependent upon the extent of liver damage, and the level of alpha2-plasmin inhibitor was closely correlated with parameters of liver functions of protein synthesis such as albumin concentration and cholinesterase activity in serum. The level of alpha2-plasmin inhibitor was fairly well correlated with the fibrinolysis inhibitor activity of serum. In contrast to alpha2-plasmin inhibitor, levels of alpha2-macroglobulin and alpha1-antitrypsin were increased significantly in liver cirrhosis. It was suggested that the reduction of alpha2-plasmin inhibitor level contributes substantially to the increased fibrinolytic activity observed in liver cirrhosis.

Adult↗
PubMed1977

The pH dependence of the resonance raman spectra and structural alterations at heme moieties of various c-type cytochromes.

The pH dependence of resonance Raman spectra were studied for ferrous and ferric cytochromes c, c2, c3, c-551, and c-555. The frequencies of the 1565 cm-1 (ferric) and 1539 cm-1 lines (ferrous) were sensitive to the replacement of the sixth ligand. The titration curve for the 1565 cm-1 line of cytochrome c was parallel with that for the 695 nm band. The pH dependence of the 1539 cm-1 line of ferrous cytochrome c3 suggested the stepwise replacement of the sixth ligand of its four hemes, although such pH dependence was not recognized for the Raman spectra of other ferrous cytochromes investigated. The relative intensities of three Raman lines at 1639, 1587, and 1561 cm-1 of ferric protoporphyrin bis-imidazole complex were changed clearly by the presence of detergents. The relative intensities of the corresponding three Raman lines of cytochromes b5 and c were close to those of the ferric porphyrin complex in the presence and absence of detergents, respectively, suggesting an appreciable difference in their heme environments. Reduced hemin in detergent solution, unexpectedly, gave the Raman spectrum of ferric low spin type.

Cytochrome c Group↗
PubMed1977

A comparison between Nitrosomas europaea and Thiobacillus novellus on the basis of their oxidation systems of inorganic compounds.

Nitrosomonas europaea and Thiobacillus novellus were compared with each other on the basis of the biochemical properties of their inorganic compound-oxidizing systems. Cytochromes c of the two organisms differ considerably from each other; N. europaea cytochrome c-552 belongs to the "bacterial-type" cytochrome c, while T. nouellus cytochrome c-550 resembles eucaryolic cytochrome c. The specificity of cytochrome oxidase for cytochrome c as the electron donor is different between the two organisms; T novellus oxidase reacts rapidly with cytochromes c of the organisms which seem to be higher than the organisms whose cytochromes c react rapidly with N. europaea oxidase. On the basis of these facts, N. europaea seems to be older organism than T. novellus in terms of evolution.

Biological Evolution↗
PubMed1977

Comparative study of the antiviral activity of acyl derivatives of 2,2'-anhydro-1-beta-D-arabinofuranosylcytosine and other nucleosides against encephalitis in mice.

Anti-deoxyribonucleic acid virus activities of 3'-O-acyl derivatives of 2,2'-anhydro-1-beta-d-arabinofuranosyl cytosine (cyclo-C) and 1-beta-d-arabinofuranosylcytosine (Ara-C) were evaluated by using an in vivo test system in mice. Among the derivatives tested, 3'-O-decanoyl cyclo-C hydrochloride was the most effective against herpes simplex virus-induced encephalitis in mice when the drug was administered directly into infected brains of mice (target-organ treatment). A comparative study of the treatment of herpetic encephalitis in mice with 3'O-decanoyl cyclo-C and other nucleosides, including Ara-C, 9-beta-d-arabinofuranosyladenine (Ara-A), and 5-iodo-2'-deoxyrudine (IUdR), proved Ara-A to be more efficacious than the other nucleosides, followed by 3'-O-decanoyl cyclo-C, which was more active than Ara-C and IUdR. Administration of 3'-O-acyl cyclo-C's by intraperitoneal injection, however, failed to demonstrate activity against herpetic encephalitis in mice. The antivaccinial activity of 3'-O-decanoyl cyclo-C was also compared with that of other compounds against encephalitis and dermal tail lesions in mice caused by vaccinia virus infection. Interaperitoneally administered 3'-O-decanoyl cyclo-C and Ara-C also showed no significant activity against the diseases. Under these test conditions, N-methylisatin-beta-thiosemicarbazone (Marboran) was the most active compound, followed by Ara-A.

Animals↗
PubMed1977

Cell-mediated immunity to measles virus in subacute sclerosing panencephalitis.

Four patients with subacute sclerosing panencephalitis were investigated for their specific cellular and humoral immunities against measles virus. Lymphocytotoxicity mediated by peripheral blood lymphocytes was evaluated with the colony inhibition test of target cells having measles antigen. The lymphocytes from two patients of subacute sclerosing panencephalitis (SSPE) specifically destroyed the carrier cells; however, no significant lymphocytotoxicity was observed in the other two patients. The result suggests the heterogeneity in cellular immune states in SSPE patients.

Adolescent↗