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Biomedical subjects

M Onishi

Publications and source records attributed to M Onishi.

At least 73 records · Page 4Linked to original sources
PubMed1982

[Mental disorders in Japanese living in Paris].

This paper relates the original work of a group of seven young Japanese psychiatrists during their residentship or their foreign assistant function in Paris. During approximately 3 years, they devoïd a part of their activity to assist their japanese copatriots who having developed some mental health accidents during they stay in the district of Paris. From the 28 patients, 15 have been hospitalized in different psychiatric wards of Paris but the french psychiatrists did not take part of the paper. The authors have divided their clinical material into 3 groups of japanese patients: tourists, permanent residents or temporary residents who represents 2/3 of the whole. In each group the incidence of nosographic diagnosis is precise and the transcultural problems are underlined. Finally, all the patients has been sent back to Japan.

Adaptation, Psychological↗
PubMed1979

Basal cell nevus syndrome. A case report.

An 11-year-old boy with multiple dentigerous cysts in the maxilla and mandible is described. Other findings seen in the face, plantar skin, skeletal system and oral cavity indicated the lesions to be due to the basal cell nevus syndrome. This was further confirmed by the presence of similar abnormalities in his father and brother.

Basal Cell Carcinoma↗
PubMed1975

Studies on the subsite structure of amylases. I. Interaction of glucoamylase with substrate and analogues studied by difference-spectrophotometry.

Studies were made on the ultraviolet difference-spectra of glucoamylase from Rhizopus niveus [EC 3.2.1.3] specifically produced by the substrate maltose and the inhibitors, glucose, glucono-1: 5-lactone (gluconolactone), methyl beta-D-glucoside, cellubiose, and cyclohexa-, and cyclohepta-amyloses. Of these, maltose and gluconolactone produced characteristic difference spectra with a trough near 300 nm. Based on studies with a model compound for a tryptophan residue, Ac-Trp, this trough was attributed to the effect of a negative charge upon the tryptophan residue. From the concentration dependency of the difference spectra, the dissociation constants of the complexes between the enzyme and maltose, glucose, and gluconolactone were evaluated to be 1.2 mM, 51 mM, and 1.5 mM, respectively. These values are in good agreement with the values of Km or K1 obtained from the steady-state kinetics. The difference-spectrophotometric data suggested that referring to the values of subsite affinities of glucoamylase, maltose, and gluconolactone occupy mainly Subsite 1, where the non-reducing-end glucose residue of a substrate is bound in a productive form and that a tryptophan residue with shows a trough near 300 nm in difference spectra is located in this subsite.

Amino Acids↗