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Biomedical subjects

A Ito

Publications and source records attributed to A Ito.

At least 919 records · Page 51Linked to original sources
PubMed1983

[Clinical studies of cefoxitin in the field of internal medicine].

Ten patients with sepsis and pneumonia complicated by leukemia or lung cancer were treated with cefoxitin (CFX) at daily dose of 6 g. The following results were obtained. 1. Clinical effects of CFX were good in 5 patients, fair in 2 and poor in 3 with effective rate of 50%. 2. Out of 8 patients with sepsis, 5 showed good response to CFX and effective rate was 62.5%. 3. Bacteriological outcomes were eradicated in 1, unchanged in 1, replaced in 2 and unknown in 6 cases. 4. Diarrhea was observed in 1 patient but this was not considered related to CFX therapy. 5. No abnormal laboratory finding due to CFX was observed. 6. It should be considered that 6 g or more of CFX is given in case of severe infections, such as sepsis or pneumonia complicated by serious underlying diseases.

Adult↗
PubMed1983

[Therapeutic effect of paromomycin sulfate on the 13th case of Mesocestoides lineatus infection found in Japan].

Mesocestoides tapeworm is a common cestode in carnivorous mammals, but human infection with the tapeworm of this genus have been infrequent. We have recently observed the 13th case of human infection with Mesocestoides lineatus in Japan. A 35-year-old man living in Gifu prefecture was admitted to our University Hospital with chief complaints of general fatigue and discharge of cestode segments in his stool. The patient gave a history of drinking blood and eating the raw liver of a snake Agkistrodon halys for medicinal purposes as same as the previous cases of all reported in Japan. The segments were identified as those of M. lineatus. He was treated orally 3 g of paromomycin sulfate. Stool examination after treatment with paromomycin sulfate revealed no evidence of parasitism. The present case may be the 2nd to have been successfully treated with paramomycin sulfate and the 21st case of Mesocestoides tapeworm infection in man described in the literature.

Adult↗
PubMed1982

Distribution of nervous system-specific forms of enolase in peripheral tissues.

The distribution of 3 forms of rat enolase (alpha alpha, alpha gamma and gamma gamma forms), including nervous system-specific forms (alpha gamma and gamma gamma), was determined in various tissues with a sensitive enzyme immunoassay system. The brain and spinal cord contained more than 100 pmol/mg protein of the alpha alpha, alpha gamma and gamma gamma enolases. Organs such as the lungs, heart, spleen, liver, and kidney contained similarly high levels of alpha alpha enolase, but these tissues contained alpha gamma and gamma gamma enolases at levels less than 1% of the central nervous tissues. High levels of the alpha gamma (greater than 10 pmol/mg) and the gamma gamma (greater than 1.5 pmol/mg) forms were found in rectum, bladder, and uterus. In gut, major portions of the nervous system-specific forms were localized in the muscle layers. Skeletal muscle and diaphragm, which are composed of striated muscle, contained low levels of 3 forms of enolase. Megakaryocytes separated from the suspension of bone marrow contained 11.3, and 0.53 amol/cell of the alpha alpha and gamma gamma enolases, respectively, with little, if any, of the alpha gamma form.

Animals↗
PubMed1982

Biosynthesis of sulfite oxidase in rat liver-determination of the site of synthesis.

The site of biosynthesis of sulfite oxidase in rat liver was determined by immunoprecipitation of nascent peptides released from ribosomes and in vitro translation products of isolated polysomes. The specificity of the immunoprecipitation of sulfite oxidase nascent peptides was confirmed by examination of the size distribution of immunoprecipitated peptides and by the competition with purified enzyme in the immunoprecipitation. Both nascent peptides analysis and the in vitro translation experiment indicated that this enzyme was mainly synthesized by free ribosomes in the cytoplasm, although bound ribosomes also contributed to the synthesis of this enzyme to some extent. When the discharge of sulfite oxidase peptides from bound ribosomes was examined with rough microsomes, however, about two thirds of the enzyme peptides synthetized by bound ribosomes were discharged to the outside of microsomal vesicles.

Animals↗
PubMed1982

Biosynthesis of sulfite oxidase in rat liver - presence of a large precursor form of the enzyme in cytosol.

The time courses of in vivo incorporation of [3H]leucine into mitochondrial, microsomal, and cytosolic sulfite oxidase were examined and it was found that the cytosol contained a precursor pool of newly synthesized sulfite oxidase which was rapidly transport into mitochondria. At 10 min after the injection of the radioactive leucine, most of the radioactivity of cytosolic sulfite oxidase was associated with the precursor whose molecular size was about 3,000 daltons larger than the authentic sulfite oxidase subunit. We concluded that sulfite oxidase was synthesized as a larger precursor in the cytosol, and transported into mitochondria to be converted to the mature enzyme. The turnover rate of the sulfite oxidase in rat liver was also determined by measuring the decay of enzyme radioactivity after the injection of [14C]leucine. Mitochondrial, microsomal, and cytosolic sulfite oxidase had an almost identical half-life of 3-4 days.

Animals↗
PubMed1982

Purification and properties of arylsulfatase C from rat liver microsomes.

Arylsulfatase C [EC 3.1.6.1] was solubilized from rat liver microsomes with Triton X-100 and purified about 2,000-fold with an overall yield of 30-40%. The purification procedure included ion-exchange chromatography, hydrophobic affinity chromatography, and gel filtration. The purified enzyme was homogeneous as judged by polyacrylamide gel electrophoresis in the presence of SDS, and its monomeric molecular weight was estimated to be about 72,000 daltons. The molecular weight of the native enzyme was about 280,000 daltons as determined by gel filtration in the presence of Triton X-100, suggesting a tetrameric structure for the enzyme molecule. The enzyme showed an isoelectric point of pH 8.1. From its strong affinity toward concanavalin A-Sepharose and colorimetric determination of neutral sugars by the phenol-sulfuric acid method, arylsulfatase C was identified as a glycoprotein. Analysis of the carbohydrates by gas-liquid chromatography demonstrated that the carbohydrate chains of arylsulfatase C were rich in mannose and N-acetyl-glucosamine, suggesting that they are the high mannose-type. This conclusion was supported by the results of digestion of the enzyme with endoglycosidase H.

Animals↗
PubMed1982

Transmembranous disposition of arylsulfatase C in microsomal membranes of rat liver.

The intramembranous disposition of arylsulfatase C [EC 3.1.6.1] was studied. The lack of stimulation by Triton X-100 of microsomal arylsulfatase C activity indicated the outside location of the active site of the enzyme in microsomal vesicles. The exposure of arylsulfatase C on the surface of microsomal vesicles was also suggested by the binding of antibodies against the purified enzyme to intact microsomes. However, larger amounts of the antibodies were bound to microsomes in the presence of a low concentration of Triton X-100, suggesting the presence of other antigenic sites of the enzyme not available to the antibodies in intact microsomes. The treatment of solubilized and microsome-bound arylsulfatase C with transglutaminase indicated two susceptible glutamine residues per subunit of the enzyme molecule. One of the glutamine residues was labeled with transglutaminase in intact microsomes, whereas the other one became available to transglutaminase only after the addition of Triton X-100 to microsomes. These observations suggested that endoglycosidase H-sensitive carbohydrate chains of arylsulfatase C are located in the lumen of microsomal vesicles. We conclude that microsomal arylsulfatase C is a transmembranous protein and exposed on both outer and inner surfaces of the membrane.

Animals↗
PubMed1982

Comparative immunochemical studies of sulfite oxidases of vertebrate livers.

1. The sulfite oxidases from various vertebrates, including rat, rabbit, chicken, frog, and eel, were partially purified and their physiochemical, kinetic, and immunochemical properties compared. The physicochemical and kinetic properties of these five enzymes were similar. 2. Antibody against the molybdenum-containing peptide prepared from purified rat liver sulfite oxidase was raised in rabbits. In Ouchterlony double diffusion and quantitative immunoprecipitation tests, the antibody could form precipitates with the enzymes from rats and rabbits, but no reaction was observed with enzymes from other sources. 3. The sulfite-cytochrome c reductase activity of the enzymes from these five animals were inhibited by the antibody, though the enzymes from chicken, frog, and eel were less sensitive to the antibody than those from rat and rabbit. 4. The inhibition of binding between 3H-labeled rat sulfite oxidase and its antibody by unlabeled enzymes from other animals demonstrated that 10 to 20% of the antibody could cross-react with these enzymes.

Animals↗
PubMed1982

Neuromuscular function and mechanical efficiency of human leg extensor muscles during jumping exercises.

The influence of prestretch amplitude on the mechanical efficiency was examined with 5 subjects, who performed 5 different series of vertical jumps, each of which differed with respect to the mechanics of the knee joint action during the prestretch (eccentric) phase of the contact on the floor. Electromyographic activity was recorded from the major extensor muscles during the entire work period of 1 min per series. In addition, expired air was collected during the test and recovery for determination of energy expenditure. Mechanical work was calculated from the vertical displacement of the body during the jumps. The results indicated that high net efficiency of 38.7% was observed in condition where amplitude of knee bending in eccentric phase was small. In large range motion the corresponding net efficiency was 30.1%. In jumps where no prestretching of extensor muscles occurred the net efficiency was 19.7%. The high efficiency of small amplitude jumps was characterized by low myoelectrical activity of the leg extensor muscles during the positive (concentric) work phase. In addition, the small amplitude jumps had shorter transition time in the stretch-shortening cycle, high average eccentric force and high stretching speed. Therefore the results suggest that the restitution of elastic energy, which was also related to the length change and stiffness of the muscles during stretch, plays an important role in regulating the mechanical efficiency of work.

Adult↗