[Case of primary hepatic tuberculosis with fever and hepatomegaly at the onset: accurate diagnosis leading to recovery].
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Biomedical subjects
Publications and source records attributed to K Wada.
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[2Fe-2S] ferredoxins isolated from various plants and algae comprise 93-99 amino acid residues and resemble each other not only in sequences, but also in physiological functions. One of them isolated from Spirulina platensis was subjected to X-ray analysis and its three dimensional structure is now known. [2Fe-2S] ferredoxins of a different type are found in halobacteria and comprise 128 amino acid residues. Both types of the [2Fe-2S] ferredoxins exhibit low redox potentials. By comparing the amino acid sequences of 28 [2Fe-2S] ferredoxins and the tertiary structure of S. platensis ferredoxin we predicted a common three-dimensional structure to the [2Fe-2S] ferredoxins and proposed a molecular surface area to be interacting with FNR. An artificial small molecule composed of 20 amino acid residues is designed on the basis of the tertiary structure of S. platensis ferredoxin. The amino acid sequence was predicted to be Pro-Tyr-Ser-Cys-Arg-Ala-Gly-Ala-Cys-Ser-Thr-Cys-Ala-Gyl-Pro-Leu-Leu-Thr Cys-Val which should have a [2Fe-2S] cluster with a low redox potential.
Purothionin from wheat flour was chemically modified by acetic or succinic anhydride under specific conditions. The complete modification of all amino groups of purothionin caused a large change in the net charge of the molecule, leading to the loss of the toxicity to mice and yeast. The sole tyrosyl residue in purothionin was nitrated by tetranitromethane at neutral pH or iodinated by the lactoperoxidase method. The nitro- and diiodo-derivatives of purothionin showed considerably reduced toxicity. Based on these modification studies we conclude that the positive charges of lysyl residues have an important role in the interaction with the negatively charged cell surface, and that the emergence of the toxicity of purothionin depends on a certain state of the tyrosyl residue.
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Cefmetazole (CMZ), a new cephamycin preparation, has been investigated to give following results. 1) Pharmacokinetics: Serum and tonsil concentration of CMZ were determined by micropore method in humans. The mean concentrations in 5 cases about 30 minutes after administration of 0.5--1.0 g intravenously were 55.4 micrograms/ml in serum, 21.7 micrograms/g in tonsil. 2) CLINICAL STUDIES: Seventy-one patients with ear, nose and throat infections were treated with CMZ receiving 1 to 6 g per day intravenously (one shot and drip infusion). Thirty-eight of 70 patients were cured excellent, 19 were good, 8 were fair and 6 were failure and effective rate was 80.3%. Adverse reaction was observed in 4 cases. Three cases showed exanthema and 1 case showed fever elevation.
Cefmetazole (CMZ) was compared to cefazolin (CEZ) for efficacy and safety in the treatment of suppurative otitis media (including acute otitis media and chronic otitis media in acute aggravating stage) under well controlled clinical trials. The therapeutic effects were analyzed statistically in 172 patients (82 administered CMZ, 90 administered CEZ). The adverse reactions were also analyzed statistically in 199 patients (CMZ 99, CEZ 100) in whom the judgement was possible. 1. The efficacy rate of CMZ (72.3% for good to excellent response) was assessed by physicians in charge to be similar to that of CEZ (59.3%). This was the same being assessed by the committee, too (CMZ 64.6%, CEZ 56.7%). 2. When patients were classified into 2 groups (acute otitis media, chronic otitis media in acute aggravating stage) with respect to diagnosis, statistically significant difference in clinical efficacy assessed by physicians in charge was observed in the cases with chronic otitis media (CMZ, CEZ). In addition, the improvements of flares on the drum membrane and the mucous membrane of eardrum were significantly better in the CMZ group than in the CEZ group. 3. Bacteriologically, 16 cases (19.8%) of S. aureus were resistant to CEZ, while only 1 case (1.2%) to CMZ. CMZ was judged to be effective in 5 of the 6 cases in which CEZ-resistant strains were detected. 4. Side effects were found in 2 cases (2.0%) treated with CMZ: one complained of retching and abdominal pain and the other developed skin eruption. On the other hand, only 1 case (1.0%) developed skin eruption in the CEZ group. These results suggest that CMZ is a new antibiotic agent which is highly valuable in the treatment of suppurative otitis media.
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This study was attempted to obtain information about biological properties of junctional acetylcholine receptor (AChR) and extrajunctional AChR, and about nerve influences on muscles AChRs under the pathological conditions of experimental myasthenia and myositis. Experimental autoimmune myasthenia gravis (EAMG) was induced in Wistar rats by immunizations with AChR purified from the electric organ of Narke Japonica without using Freund's complete adjuvant experimental myositis by immunization with rat muscle extract depleted of AChR. Thirty-five days after the initial immunization, unilateral dissection of the ischiadic nerve was performed in all immunized rats. Contents of AChR in both hind limb muscles were measured by double immunoprecipitation assay method 15 days after the experimental denervation. In the control animals the amount of AChR extractable from innervated muscles was 2.7 +/- 0.5 (mean +/- s.d.) pmole/g muscle and increased about 10-fold 15 days after the denervation (30 +/- 7.9). In rats with EAMG, AChR contents was reduced in both denervated (1.1 +/- 1.0) and innervated muscles (1.3 +/- 0.9). In experimental myositis, the increase of muscle AChR was impaired in denervated muscles (2.4 +/- 0.6), but AChR contents was not reduced in innervated muscles (2.7 +/- 0.9). These results suggest that nerves may influence AChR metabolism, keeping numbers of AChR constant even in inflammatory condition. In addition, germinal centre formation in thymic medulla was detected in EAMG rats.
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A [2Fe-2S] ferrodoxin from Spirulina platensis crystallized in space group C2221 with cell dimensions of a = 62.32, b = 28.51, c = 108.08 A, and alpha = beta = gamma = 90.0 degrees. X-ray structure analysis of the protein was carried out at 2.5 A resolution by the single isomorphous replacement method coupled with the derivative and the native anomalous dispersion methods. Phase angles of 2182 independent reflections were determined and their average figure of merit was 0.58. Each of 98 residues was superposed on the electron density sections enlarged to 2 cm/l A with a half-mirror device (Richards box). About 25% of the total residues form beta-structure and 10% fold in a tow-turn alpha-helix. A beta-barrel-like structure was found in the main chain fold. A polypeptide segment from residues 41 to 49 forms a loop structure outside the barrel. Two iron atoms of the [2Fe-2S] cluster are coordinated by three cysteines in the loop and by Cys-79. Hydrogen bonds of NH....S and OH....S stabilize the loop conformation. Most side chains are reasonably oriented in the molecule. The internal volume of the barrel is occupied by aliphatic nonpolar residues. All the charged groups are accessible to solvent molecules.