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Biomedical subjects

M Tashiro

Publications and source records attributed to M Tashiro.

At least 253 records · Page 14Linked to original sources
PubMed1980

Monitoring perinatal mortality rates: California, 1970 to 1976.

Recent developments have emphasized the need to monitor perinatal mortality statistics by small geographic areas. A method is presented which separates county-specific perinatal mortality rates into a component reflective of socioeconomic, behavioral, and environmental variables, and a component that relates more directly to hospital-based intra- and postpartum care. Major differences in geographic variations were observed between the crude rate and the two components. An arbitrary index of the need for perinatal health services was created by combining the two components with the number of perinatal deaths in each county. Although there are some obvious limitations, the index serves as a useful guidepost for monitoring perinatal mortality on a statewide basis.

Bayes Theorem↗
PubMed1980

Pigmented contact dermatitis from azo dyes. I. Cross-sensitivity in humans.

Eight patients suffering from pigmented contact dermatitis caused by the commerical Brilliant Lake Red R were patch tested with purified Sudan I and its several chemical analogues. Positive reactions were observed to Sudan I, Orange SS, Brilliant Lake Red R, Vacanceine Red, Yellow OB and Sudan II. Negative tests were obtained with Toluidine Red, Permanent Orange, Lithol Red and Sudan III. We found that the commerical Brilliant Lake Red R which has been said to be most important causative agent of pigmented contact dermatitis, contained Sudan I as a major impurity. The patients reacting to Brilliant Lake Red R always gave a positive reaction to Sudan I, but those reacting to Sudan I did not always give a positive reaction to Brilliant Lake Red R. This suggests that Sudan I is a potent sensitizer and may induce contact sensitivity and Brilliant Lake Red R itself is a weak sensitizer or a cross-reacting substance.

Adult↗
PubMed1980

The position of the reactive site peptide bond in eggplant trypsin inhibitor molecule.

The purified trypsin inhibitor from eggplant (Solanum melongena, L.) has an Arg-X bond in the reactive site which is selectively cleaved by limited hydrolysis with a catalytic amount of bovine trypsin. So-called trypsin-modified inhibitor was separated from the native one by QAE-Sephadex A-25 chromatography. After the cleavage of disulfide bonds of isolated modified inhibitor by means of reduction and S-carboxymethylation, two fragments (F-I and F-II) were obtained by gel filtration on Sephadex G-25. F-I and F-II were composed of 44 and 14 amino acid residues, respectively. The sum of both coincided with that of the native inhibitor. The N-terminal of F-I was blocked and the C-terminal was arginine. In F-II, the N-terminal was identified as asparagine and the C-terminal as serine. No N-terminal amino acid could be detected in the native inhibitor, as described in our previous paper (7). Therefore, it is concluded that the reactive site of eggplant trypsin inhibitor is an arginylasparagine bond located between residues 44 and 45.

Amino Acids↗
PubMed1979

Brilliant Lake Red R as a cause of pigmented contact dermatitis.

Twenty-three patients suffering from pigmented contact dermatitis caused by cosmetics containing Brilliant Lake Red R were observed. Commercial samples of Brilliant Lake Red R proved to contain many ethyl acetate extractable impurities; 1-phenylazo-2-naphthol and azobenzene were isolated and identified. To determine the responsible allergens, five patients were examined by patch tests with purified samples of azo-dyes and the unidentified fractions of ethyl acetate extractable impurities. Three out of five showed weaker reactions to purified samples of Brilliant Lake Red R and the other two showed equal reactions compared to the commercial product. 1-Phenylazo-2-naphthol was found to be a strong allergen in all cases but none showed a positive reaction to azobenzene. Some unidentified fractions also gave positive results. Patch tests were performed with 4-phenylazo-1-naphthol, 4-phenylazo-1-naphthol-2-carboxylic acid, and 2,4-bis(phenylazo)-1-naphthol, as structurally related compounds derived from 1-naphthol. All gave negative and they were not detected in the ethyl acetate extractable impurities by thin-layer chromatography.

Adult↗
PubMed1979

Factors influencing the release of renin in patients under chronic dialysis treatment.

Plasma renin activities (resting PRA, post-dialysis delta PRA) were studied in 61 patients under chronic dialysis treatment. Removed sodium and removed water were estimated at each dialysis. Delta PRA/removed-sodium and delta PRA/removed-water were calculated as indices in response to the removal of sodium and water during the dialysis. 1)Resting PRA (pre-dialysis PRA) was positively correlated to delta PRA/removed-sodium, delta PRA/removed-water, serum osmolality, and diastolic blood pressure, but negatively to serum sodium concentration, age, and pulse pressure/diastolic blood pressure. Statistically significant factors controlling the resting PRA were delta PRA/removed-sodium, delta PRA//removed-water, and serum sodium concentration. Resting PRA was slightly correlated to diastolic blood pressure and age. 2)Post-dialysis PRA was significantly correlated to the resting PRA, delta PRA/removed-sodium, delta PRA/removed-water, serum sodium concentration, and age, but not to the blood pressure indices.

Adolescent↗
PubMed1979

Purification and characterization of a trypsin inhibitor from rice bran.

A trypsin inhibitor was isolated and purified from the bran of rice, Oryza sativa, by extraction with 1% sodium chloride, heat treatment, ammonium sulfate precipitation, ion-exchange chromatography on a CM-Sephadex C-25 and gel filtration on a Sephadex G-75. The final preparation was homogeneous by electrophoretic analysis. Rice bran trypsin inhibitor (RBTI) had a molecular weight of about 14,500 and an isoelectric point of 8.07. The amino acids, acid composition was characterized by high contents of basic amino acids, aspartic acid, glutamic acid, proline and cystine. BRTI inhibited bovine trypsin at an inhibitor-enzyme molar ratio of 1:1.6. It displayed, however, nobility to inhibit alpha-chymotrypsin, pepsin, papain and subtilisin BPN'.

Amino Acids↗
PubMed1979

[Clinical experience with NK 631 in malignant tumors of skin (author's transl)].

NK 631, a new derivative of bleomycin, was clinically used in 14 cases of malignant tumors of skin. The results obtained were remarkably effective in 7 cases, effective in 3 cases, slightly effective in 2 cases and ineffective in 2 cases. The effective ratio was 71% when calculated regarding slightly effective as ineffective. Compared with bleomycin, we were impressed that the side effects observed with NK 631 were similar to those with bleomycin, but the influences for lung were smaller and slighter than the latter.

Adult↗
PubMed1977

An improved method for the purification of eggplant trypsin inhibitor.

The trypsin inhibitor in eggplant, Solanum melongena L., was isolated and purified by the improved method with the techniques of dialysis using acetylated cellulose tube and ion-exchange chromatography on DEAE-Sephadex. The final preparation was found to be homogeneous by disc and SDS-polyacrylamide gel electrophoresis. This inhibitor had the molecular weight of about 6,200, the pI value of 4.7, and furthermore characteristic amino acid composition lacking in tryptophan, histidine, valine and methionine. The trypsin inhibition data indicated that the purified inhibitor combined with bovine trypsin [EC 3.4.21.4] in the molar ratio of 1:1. These properties of this inhibitor were in agreement with those of the dialyzable eggplant trypsin inhibitor previously purified, indicating that the dialyzable and non-dialyzable inhibitors in eggplant are identical.

Amino Acids↗
PubMed1976

Purification and partial characterization of a protein proteinanse inhibitor isolated from eggplant exocarp.

A protein proteinase inhibitor was isolated and purified from eggplant exocarp by heat treatment, ammomium sulfate fractionation, column chromatography on DEAE-cellulose, and gel filtration on Sephadex G-25 and G-50. The final purified preparation of the inhibitor was found homogeneous by electrophoretic analysis. The inhibitor showed strong and stoichiometric inhibition on trypsin whereas it showed weak inhibition on alpha-chymotrypsin. It displayed no inhibiting characteristics on pepsin. The molecular weight of the inhibitor was estimated to be approximately 6000. This finding, with the trypsin inhibition data, suggested that the inhibitor combined trypsin in the molar ratio of 1:1. The amino acid analysis indicated that the inhibitor is rich in half-cystine, glycine and aspartic acid, and contains no tryptophan, histidine, methionine or valine.

Amino Acids↗
PubMed1976

The reactive site of eggplant trypsin inhibitor.

The reactive site peptide bond of the eggplant inhibitor against trypsin [EC 3.4.21.4] was identified by chemical modifications with 1,2-cyclohexanedione, 2,4,6-trinitrobenzenesulfonic acid, acetic anhydride and glyoxal, and by sequential treatments with trypsin and carboxypeptidase B [EC 3.4.12.3]. The inhibitor was significantly inactivated by chemical modifications of arginine residues, but was not affected by lysine modifications. Free arginine was released from the trypsin-modified inhibitor by carboxypeptidase B digestion, accompanied by a marked loss of inhibitory activity. A serine residue was newly exposed at the N-terminal amino acid of the inhibitor after modification with trypsin. The reactive site of the inhibitor against trypsin was concluded to be an arginylseryl bond. The inhibitor was completely inactivated by full reduction of its disulfide bonds.

Anhydrides↗
PubMed1975

Occurrence of a trypsin inhibitor in eggplant exocarps.

A trypsin inhibitor was extracted from eggplant exocarps with several buffers. The 0.1 M acetate buffer, pH 5.5. extract had the highest specific activity. The crude inhibitor, obtained by heat treatment and salting-out from the acetate buffer extract, contained 4.5% nitrogen and 22.6% hexose. Isoelectrofocusing demonstrated that this crude inhibitor in the eggplant exocarps was composed of at least three forms, one of which differed in its isoelectric point. The form at pH 4.7 had the strongest activity. The molecular weights of these inhibitors were estimated to be between 5,000-10,000 by gel filtration.

Chemical Phenomena↗