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Biomedical subjects

Y Shimamori

Publications and source records attributed to Y Shimamori.

At least 19 recordsLinked to original sources
PubMed1999

[Dispersal of pollen and the variation in number of patients prescribed medicine for allergies in Otaru].

The number of patients prescribed medicine for allergies increased in May and September. Therefore, we suspected that the cause for the increase was pollen. Many kinds of pollen occur in Otaru, such as alder in April, Japanese black pine, white birch, acacia, larch in May, oak in June, and mugwort in September. The total number of pollen count of white birch was about 9 times that of mugwort, but the total number of patients prescribed Celestamine in the season of white birch pollen was about 0.8 times that of mugwort pollen. These results seen in Otaru differed from those in neighboring Sapporo. The coefficient of the correlation of the number of mugwort and white birch pollen and those of patients prescribed Celestamine were r = 0.304 and r = 0.766, respectively. We believe that making available information on pollen is very useful to improve the quality of life of patients.

Air Pollutants↗
PubMed1999

[Economical evaluation for drug consultation at home].

We started drug consultation at patients' homes in October, 1998. The number of drug consultations are 2.65 per month per patient and the consulting time is 2.25 hours per patient. The fee for drug consultation is 550 points twice a month. We evaluate the fee for drug consultation. Our data suggest that this fee needs to be 550 points three times a month.

Aged↗
PubMed1997

Comparison of the hydrolysis of the three types of natriuretic peptides by human kidney neutral endopeptidase 24.11.

The degradation of 3 human natriuretic peptides by human kidney neutral endopeptidase 24.11 has been investigated. The studies revealed that hANP-28 and hCNP-22 are the preferred substrates, whereas hBNP-32 is not. The enzyme has been known to inactivate hANP-28 from cleavage at the Cys-Phe bond at the beginning of its ring structure. Analysis of the cleavage sites of each peptide indicated that the initial cleavage site of hCNP-22 is analogous to that of hANP-28. The Cys-Phe bond of hBNP-32 was insensitive to this enzymatic cleavage. We speculate that the stability of hBNP-32 may result from the insusceptibility of its Cys-Phe bond at the beginning of the ring structure.

Amino Acid Sequence↗
PubMed1995

Characterization of gelatinases in human placenta.

Matrix metalloproteinases were extracted from human placenta. Gelatin zymograms showed four bands with gelatinase activity. These four bands were detected at Mr 72,000, 92,000, 130,000, and 210,000 respectively. Reduced and alkylated samples were detected at Mr 72,000 and 92,000. Immunoblotting analysis showed that the enzymes of Mr 130,000 and 210,000 were derived from gelatinase B (EC 3.4.24.35). Also, reduced gelatinase was activated by 4-aminophenylmercuric acetate more readily than a nonreduced gelatinase. This indicates that human placental gelatinases are stabilized by the tissue inhibitor of metalloproteinases.

Alkylation↗