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Biomedical subjects

M Ozeki

Publications and source records attributed to M Ozeki.

At least 109 records · Page 6Linked to original sources

An in vitro study on the toxoplasmacidal activity of lonomycin A in host cells.

Lonomycin A at various concentrations was tested for its inhibitory effect on Toxoplasma multiplication in host cells cultured in vitro. Results indicate that lonomycin A at a concentration of 0.01 micrograms per ml in TC-199 medium demonstrated a high degree of antitoxoplasma activity with complete inhibition of Toxoplasma multiplication in the host cells. Lymphokines, a supernatant produced from spleen cells of mice infected chronically with Toxoplasma gondii, inhibited Toxoplasma multiplication in mice macrophage and kidney cell monolayers. However, lonomycin A inhibited completely Toxoplasma multiplication in non-specific cells, i.e. not only in mice macrophages and kidney cells but also in cells of human and other animal species.

Animals↗

Additive protection of aprotinin, protease inhibitor to cold cardioplegia from ischemic myocarium.

Protective action of aprotinin froom ischemic myocardial damage was evaluated in 9 patients compared to non-treated 18 patients, who underwent open heart surgery (22 ACB, 3 AVR and 2 MVR) with respect to the alterations of beta-glucronidase, acid-phosphatase, MB-CPK and m-GOT. Cold cardioplegia with glucose-insulin-potassium solution was used in this investigation. Average arrest time was 78.6 +/- 4.9 minutes associated with hypothermia between 25 and 28 degrees C in rectal temperature. Aprotinin was administered in 9 patients intravenously with 5,000 KIU/Kg 30 minutes prior to CPB and then 5,000 KIU/Kg in the prime solution. Activity of beta-glucronidase was significantly suppressed in the aprotinin-treated group compared to the non-treated group following cardioplegia and in the reperfusion period up to 6 hours, however, acid-phosphatase failed to demonstrate significant difference among two groups. Serum MB-CPK and m-GOT levels in the aprotinin-treated group did not elevate the beginning of reperfusion following cardioplegia. These data suggest that aprotinin add myocardial protection to cold cardioplegia.

Acid Phosphatase↗

Lonomycins B and C, two new components of polyether antibiotics. Fermentation, isolation and characterization.

Lonomycin B (II), C44H75O14Na, m.p. 181-182 degrees C, and lonomycin C (III), C43H73O14Na, m.p 186-187 degrees C, were isolated as their sodium salts from the fermentation broth of Streptomyces ribosidificus TM-481. Their physicochemical properties demonstrated that II and III are closely related congeners of lonomycin A (I). The identical mass spectra of methyl esters of I and II indicated that II is a stereoisomer of I. On the other hand, the mass spectrum of a methyl ester of III showed a peak at m/e 810 due to M+-H2O which is smaller by 14 mass units than the maximum peak at m/e 824 due to M+-H2O of the methyl esters of I and II. This result together with the elemental analysis strongly suggested that III is a demethyl derivative of I or II. II and III are slightly less active than I in their antimicrobial activities.

Anti-Bacterial Agents↗

Studies on the ionophorous antibiotics. XXIV. Leuseramycin, a new polyether antibiotic produced by Streptomyces hygroscopicus.

A new antibiotic leuseramycin has been isolated from the cultured mycelium of the strain of Streptomyces hygroscopicus TM-531. Physicochemical data, in particular those of 1H- and 13C-NMR spectra, revealed that leuseramycin is closely related to dianemycin in its structure, the former having a methyl group in place of the hydroxymethyl group at C-30. It is active against Gram-positive bacteria, some phytopathogenic fungi and some protozoa.

Anti-Bacterial Agents↗