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Biomedical subjects

E Ono

Publications and source records attributed to E Ono.

At least 145 records · Page 8Linked to original sources
PubMed1983

Pancreatic and salivary amylase determination using a short-chain chromogenic substrate (alpha-4-nitrophenyl-maltoheptaoside) and an amylase inhibitor.

We describe a simple method to determine serum amylase isoenzyme activity with alpha-4-nitrophenyl-maltoheptaoside as substrate and the use of an amylase inhibitor. Day-to-day reproducibility (CV) was 2% for total amylase, 3-5% for pancreatic and salivary amylase; within-day precision was 1% for total amylase, 1-4% for pancreatic and salivary amylase. The concentrations of total, pancreatic and salivary amylase were determined in 169 sera obtained from healthy adults (82 men and 87 women). Total, pancreatic and salivary amylase concentrations in males were respectively 184, 105 and 66; in females 210, 97 and 92 U/l (mean). Our method is simple and rapid; our results agree well with those of other authors, who have used electrophoretic or blue starch methods.

Adult↗
PubMed1982

Asplenia and polysplenia syndrome.

This report described the morphological characteristics of seven cases of asplenia syndrome and three of polysplenia syndrome. Each syndrome has been characterized by a tendency for symmetric development of normally asymmetric organs, with varying degrees of cardiovascular anomalies. These latter anomalies are usually present in asplenia syndrome to a greater extent than in polysplenia syndrome. While, as observed in our material, the conotruncal anomalies were present more commonly in cases with asplenia, and absence of inferior vena cava with azygos continuation was seen specifically in all the cases with polysplenia. This evidence implied the presence of some pathogenetic distinction between the two syndromes.

Abnormalities, Multiple↗
PubMed1982

Production and characterization of monoclonal antibodies to lipopolysaccharide antigen of Leptospira interrogans serovar kremastos and canicola.

Monoclonal antibodies to Leptospira interrogans were provided by cell fusions between a myeloma cell line, P3/X63-Ag8.653, and spleen cells of BALB/c mice immunized with two different leptospiral lipopolysaccharide antigens. One antigen was prepared from Leptospira interrogans serovar kremastos strain Kyoto and the other from serovar canicola strain Hond Utrecht IV. Eighteen hybridoma cell lines secreting monoclonal antibodies to the former organisms and five hybridoma cell lines secreting monoclonal antibodies to the latter organisms were established during 6 month cultivation. On the basis of their microscopic agglutination reactivities, 18 anti-kremastos Kyoto monoclonal antibodies were classified into 10 distinct groups, and 5 anti-canicola monoclonal antibodies into 3 distinct groups.

Agglutination Tests↗
PubMed1981

Inhibition of Leptospiricidal reaction by the type-specific main antigen of Leptospira.

The serovar-specificity of the leptospiricidal activity test mediated by antiserum and complement was demonstrated by the fact that the leptospiricidal activity of the antiserum against the serovar-specific main (TM) antigen of copenhageni shibaura and the antiserum against the whole cells of the same strain were inhibited by the homologous but not the heterologous TM antigens. The inoculation of TM antigen produced in a rabbit the antibodies which react in the leptospiricidal activity test. These results may also show that the substance which participates in the leptospiricidal activity test may be the TM antigen.

Animals↗
PubMed1979

Muscular form of glycogenosis type II (Pompe's disease).

An 11-year-old boy who was previously thought to have progressive muscular dystrophy was studied clinically, biochemically, and histologically. He was seen initially with an amyotonic syndrome with no clinical evidence of heart disease. Light and histochemical examination showed vacuolar degeneration and abnormal accumulation of glycogen in the muscular fibers. Electron microscopy showed aggregates of glycogen granules surrounded by a well-defined membrane, as in previously reported cases of type II glycogenosis. Enzymatic study disclosed that acid alpha-glucosidase was deficient in muscle, liver, and heart tissue, although neutral alpha-glucosidase was present within normal ranges. Measurement of acid and neutral alpha-glucosidase activity in muscle from the patient and his sisters and in urine from them and their parents indicated that his sisters are heterozygotes and his parents probably are heterozygotes. The disease was transmitted as an autosomal-recessive trait.

Child↗
PubMed1977

Properties of the alpha-glucosidase from various human tissues in relation to glycogenosis type II (Pompe's disease).

The physico-chemical and electrophoretical properties of alpha-glucosidases from various human tissues and urine have been studied. There were some differences among Peak I enzymes (neutral alpha-glucosidases) obtained from liver, heart, muscle, kidney and urine. These differences are based on different effects of tris(hydroxymethyl)aminomethane and various thermostabilities of the Peak I enzymes. Electrophoretically, the Peak I enzyme activity at pH 6.5 from control tissues displayed a two-banded pattern except in kidney and urine. In the patient with the adult form of Pompe's disease the faster band of the Peak I enzyme from heart and muscle was not found and the slower band of the Peak I enzyme from liver was more cathodic. The results are discussed in relation to glycogenosis type II (Pompe's disease).

Copper↗
PubMed1977

Urinary alpha-glucosidase analysis for the detection of the adult form of Pompe's disease.

Two alpha-glucosidases from human heart, liver, muscle, kidney and urine have been separated by means of Sephadex G-100 gel filtration. The first peak (Peak I) was neutral alpha-glucosidase and the second peak (Peak II) was lysosomal acid alpha-glucosidase. Peak II was absent in a patient with the adult form of Pompe's disease. KCl stimulated the activity of the Peak II enzyme but it strongly inhibited the activity of the Peak I enzyme measured at pH 4.0. Decreases in the urinary alpha-glucosidase activity measured at pH 4.0 with added KCl and the ratio of the activity at pH 4.0 with added KCl/the activity at pH 6.5 without KCl may aid in the detection of homozygotes or heterozygotes with the adult form of Pompe's disease.

Adolescent↗