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Biomedical subjects

C Shimizu

Publications and source records attributed to C Shimizu.

At least 127 records · Page 7Linked to original sources
PubMed1987

Purification and characterization of Vibrio vulnificus protease.

A protease was purified from a strain of Vibrio vulnificus isolated from the blood of a septicemic human. The vibrio was cultured in bacto peptone-yeast extract medium, and the protease was purified by a purification procedure including ultrafiltration of the culture supernatant with an Amicon YM 5 membrane, diethylaminoethyl-Sephacel column chromatography, Sephacryl S-200 column chromatography and fast protein liquid chromatography on Mono Q column. The protease preparation revealed homogeneity on polyacrylamide gel electrophoresis and about 30,000-fold purification was achieved, with a yield of about 30%. The isoelectric point of the purified V. vulnificus protease was about 5.80 and its molecular weight was ca. 45,000 by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The optimum pH of the protease activity was 8.0. The V. vulnificus protease was inhibited by a metalloprotease inhibitor and zinc ion and/or ferrous ion were essential for its enzyme activity. No cysteine residue was detected in the V. vulnificus protease. The protease had caseinolytic, elastolytic and collagenolytic activities.

Amino Acids↗
PubMed1987

[The clinical value of sialyl SSEA-1 antigen in patients with gynecologic tumors].

In order to estimate the clinical significance of sialyl SSEA-1 antigen, the antigen was measured with an "FH-6" Otsuka Kit in sera from patients with various gynecologic tumors. Among the patients with uterine malignancies and benign ovarian tumors, the incidence of elevated sialyl SSEA-1 antigen levels was very low. However, among the patients with ovarian malignancies, serum sialyl SSEA-1 antigen was significantly increased in the following order: clinical stage I (40%), stage II (67%) and stage III (75%). The serum antigen values were also correlated with the effect of treatment. In addition, high antigen values were also observed in all 14 malignant ovarian cyst fluids tested. The immunohistochemical localization of sialyl SSEA-1 antigen was determined by an immunoperoxidase method using FH-6 monoclonal antibody. A weak positive reaction was observed in normal glands of female genital tracts. However, the intense staining was shown on the mocus materials or on the luminal surface of some malignant glands as well as in the cytoplasm of some adenocarcinoma cells of gynecologic malignancies, although there were few positive cases or positive cells. Thus, sialyl SSEA-1 antigen appears to be a useful marker in the diagnosis of ovarian malignancies.

Adenocarcinoma↗
PubMed1986

DNA strand scission by hemin-thiolate complexes as models of cytochrome P-450.

Hemin-thiolate complexes, as chemical models for cytochrome P-450 monooxygenases, have been shown to cause strand scission of DNA. Circular super-coiled DNA was degraded to open-circular and linear forms by these complexes in 30 min at pH 7.8 under aerobic conditions, the degradation depending on the structure of the thiol ligand and the ratio of thiol ligand to hemin concentration. The relationship between the structure of the thiol ligand and DNA strand cleaving activity was examined. Complete cleavage of DNA was observed by complexes containing TGE and ME at 400-600 moles excess of thiol ligand to hemin, those containing Cys, CysMe, and CysEt at 50-200 moles excess, and those containing MPG, GSH, penta- and nona-peptides at 5-20 moles excess. Complexes containing NACys and MEA caused no cleavage of DNA. Inhibition experiments suggested the involvement of active oxygen species in the cleavage.

Cysteine↗
PubMed1984

Effects of nicardipine and other Ca2+-antagonists on catecholamine transport into chromaffin granule membrane vesicles.

Nicardipine (10(-7)-2 X 10(-5) M) inhibited the transport of noradrenaline into chromaffin granule membrane vesicles in a concentration-dependent manner. This inhibitory effect of nicardipine was found to be appreciably stronger than that of other Ca2+-antagonists(diltiazem, nifedipine and verapamil) and was not due to the blockade of Ca2+-channel in the granule membranes.

Animals↗