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Biomedical subjects

E Amano

Publications and source records attributed to E Amano.

11 recordsLinked to original sources

[A case of renal oncocytoma with cystic formation].

A 60-year-old man was admitted to our hospital because of a right renal mass incidentally detected by ultrasonography during a general health check. Computerized tomography (CT) and magnetic resonance imaging (MRI) revealed a solid mass measuring 6 cm diameter containing a cystic portion in the right kidney. Cystic renal cell carcinoma was suspected, and right nephrectomy was performed. The gross appearance showed a well circumscribed mahogany brown tumor in the lower portion. On cross section of the tumor, a solid mass was seen in the cystic portion. Microscopically, oncocytic cells with eosinophilic granular cytoplasm were scattered on the cystic wall, and tumor cells formed microcystic structures in the solid part. Therefore, the tumor was diagnosed as renal oncocytoma with cystic formation. Only twelve cases have previously been reported in the literature.

Adenoma, Oxyphilic↗

Flow system for automated analysis of maize pollen.

Pollen grains are haploid gametes of uniform shape and size, and can be obtained in large quantity. If appropriate traits are used, they can be an excellent material for investigation of rare but important biological events like intracistronic recombinations or mutations induced by very low level of mutagens. This advantage will be further improved, if the laborious counting and examination can be made automatically. For automation of pollen analysis, techniques of flow analysis and image analysis would be applicable. Flow analysis with a optical detector was tested using maize pollen. Pollen grains were transported by gentle suction through a glass capillary which was placed under a microscope. Interruptions of the light path by pollen grains were detected by a silicon photocell after optical magnification and converted into electric pulses. The frequency distribution of pulse height was examined by a multichannel pulse height analyzer. 10(6) pollen grains would be counted and classified within about 30 min for a pollen suspension dilute enough for separation of each pulse. The flow system tested seems promising for detection of Wx mutant pollen in a wx pollen population after iodine staining if illumination of sample particles is improved.

Amylose↗

Genetic and biochemical characterization of waxy mutants in cereals.

During fine structure analyses of artificially induced waxy mutants in maize by use of Nelson's pollen analysis methods, it was noticed that some mutants showed a phenotype intermediate between waxy and normal nonwaxy. Such intermediate or leaky waxy mutants were frequent among mutants induced by a chemical mutagen, EMS. They seemed to be located evenly within the waxy locus. This would suggest that they might have been missense mutations, which would produce full-sized but partially inactivated enzymes, rather than deletions or frameshift mutations. To confirm the intermediate phenotype, a rapid measuring system was developed to measure waxiness of endosperm quantitatively. It was based on the blue value method and is applicable to a single grain of rice. Among the 27 waxy mutant lines of maize, including 11 EMS-induced, two of the EMS-induced mutants were clearly intermediate. Eighteen EMS induced wx mutants of rice were also examined, and nine were intermediate.

Alleles↗

Guanylate cyclase in neuroblastoma N1E 115 cells: presence of endogenous activator.

Guanylate cyclase in cultured neuroblastoma N1E 115 cells was readily solubilized. MgCl2 as well as MnCl2 served as a metal cofactor of the guanylate cyclase. The maximal guanylate cyclase activity obtained with MgC12 was 80% of that with MnCl2. When the supernatant of cell homogenate was adjusted to pH 5.2, all of enzyme activity was precipitated. The guanylate cyclase activity recovered in the pH 5.2 precipitate was reduced to about 10% of the original supernatant. Combination of the pH 5.2 supernatant and precipitate fractions, however, restored guanylate cyclase activity, indicating that the pH 5.2 supernatant contains an endogenous activator for guanylate cyclase. The activating factor in the pH 5.2 supernatant remained in the aqueous phase after proteins were removed by perchloric acid. The factor was filterable through Diaflo ultrafilter membranes UM 2 and UM 10 indicating that the factor is a small molecule. The activation by the endogenous activator was prevented by N-methylhydroxylamine and lysolecithin.

Cell Fractionation↗

Evaluation of the DuPont aca amylase method.

The dilution/activity curve for the DuPont aca kinetic amylase (EC 3.2.1.1) method is linear to approximately six times the upper limit of the expected range. Total reaction time on the aca is 4.3 min; however, there is a nonlinear rate of change in absorbance for at least the first 8 min, which is consistent with a lag phase. The within-run and day-to-day coefficients of variation were 2.4% at 100 U/L and 3.6% at 114 U/L, respectively. There was no interference by marked hemolysis (hemoglobin 4 g/L) or by glucose concentrations of 10--50 g/L. Comparisons by the split-sample method between the Amylochrome procedure and the aca procedure gave correlation coefficients of 0.992 for serum and 0.989 for urine. A second comparison, between the AutoAnalyzer I method and the aca, gave correlation coefficients of 0.998 for serum and 0.909 for urine. The expected range for serum was 18--106 U/L and for urine 2--33 U/2 h.

Amylases↗

Subcellular distribution and activation by non-ionic detergents of guanylate cyclase in cerebral cortex of rat.

Non-ionic detergents stimulated particulate guanylate cyclase activity in cerebral cortex of rat 8- to 12-fold while stimulation of soluble enzyme was 1.3- to 2.5-fold. Among various detergents, Lubrol PX was the most effective one. The subcellular distribution of guanylate cyclase activity was examined with or without 0.5% Lubrol PX. Without Lubrol PX two-thirds of the enzyme activity was detected in the soluble fraction. In the presence of Lubrol PX, however, two-thirds of guanylate cyclase activity was recovered in the crude mitochondrial fraction. Further fractionation revealed that most of the particulate guanylate cyclase activity was associated with synaptosomes. The sedimentation characteristic of the particulate guanylate cyclase activity was very close to those of choline acetyltransferase and acetylcholine esterase activities, two synaptosomal enzymes. When the crude mitochondrial fraction was subfractionated after osmotic shock, most of guanylate cyclase activity as assayed in the absence of Lubrol PX was released into the soluble fraction while the rest of the enzyme activity was tightly bound to synaptic membrane fractions. The total guanylate cyclase activity recovered in the synaptosomal soluble fraction was 6 to 7 times higher than that of the starting material. The specific enzyme activity reached more than 1000 pmol per min per mg protein, which was 35-fold higher than that of the starting material. The membrane bound guanylate cyclase activity was markedly stimulated by Lubrol PX. Guanylate cyclase activity in the synaptosomal soluble fraction, in contrast, was suppressed by the addition of Lubrol PX. The observation that most of guanylate cyclase activity was detected in synaptosomes, some of which was tightly bound to the synaptic membrane fraction upon hypoosmotic treatment, is consistent with the concept that cyclic GMP is involved in neural transmission.

Animals↗