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Biomedical subjects

M Terao

Publications and source records attributed to M Terao.

At least 109 records · Page 6Linked to original sources
PubMed1979

Herbicidins F and G, two new nucleoside antibiotics.

A mutant of Streptomyces saganonensis No. 4075, obtained with N-methyl-N'-nitro-N-nitrosoguanidine treatment, produced herbicidins F and G without herbicidins A and B. Isolation of the antibiotics was performed by adsorption on resinous adsorbent followed by elution with aqueous MeOH. Herbicidin F was obtained as colorless needles after extraction of the eluate using methylene dichloride. Purification of herbicidin G was completed with silica-gel chromatography to give a crystalline powder. physico-chemical characterization revealed that herbicidins F and G were new nucleoside antibiotics having an adenine moiety in their structures. There was no inhibition activity at 100 micrograms/ml of herbicidins F and G against all of bacteria and yeast tested. Herbicidin F, as well as herbicidin G, are inhibitory activity against some of fungi such as Tricophyton rubrum (MIC; 6.25 micrograms/ml), T. asteroides (6.25 micrograms/ml), T. mentagrophytes (6.25 approximately 12.5 micrograms/ml), Botrytis cinerea (12.5 micrograms/ml), Blastomyces brasiliensis (12.5 approximately 25 micrograms/ml).

Animals↗
PubMed1978

Membrane-bound arylamidase from human hepatoma cells having the same electrophoretic mobility as placental membrane-bound arylamidase.

A membrane-bound arylamidase from well-differentiated hepatocellular carcinoma having the same electrophoretic mobility as placental membrane-bound arylamidase was found. The enzyme was found to be a sialoprotein and was activated by Co2+. Hepatoma membrane-bound arylamidase had a similar molecular weight (240 000) and kinetic properties to normal liver membrane-bound arylamidase, but differed from the liver enzyme with respect to electrophoretic mobility, heat stability and urea inactivation.

Aminopeptidases↗
PubMed1978

Selective Growth Inhibition of Sphaerotilus natans and Beggiatoa sp. by Nucleosides.

9-beta-d-Arabinofuranosyladenine (ara-A) has been found to specifically inhibit the growth of Sphaerotilus natans and Beggiatoa sp. at a low concentration (0.78 mug/ml). The nucleoside had no antimicrobial activity against various microorganisms other than Candida albicans at 1,000 mug/ml. 3'-Deoxyadenosine, 2'-deoxyadenosine, formycin, and some derivatives of ara-A also showed inhibitory activity against Sphaerotilus natans. The growth of Beggiatoa sp. was also inhibited by 9-beta-arabinofuranosylhypoxanthine, 3'-deoxyadenosine, 2'-deoxyadenosine, formycin, toyocamycin, tubercidin, and some derivatives of ara-A. ara-A was quite stable in water and had no harmful effect on fish at 200 mug/ml. The possible uses of ara-A and some nucleosides in controlling the proliferation of S. natans and Beggiatoa sp. in the environment are discussed.

Journal Article↗
PubMed1977

Placental form of membrane-bound neutral arylamidase found in renal cell carcinoma.

A placental form of membrane-bound neutral arylamidase was found in the tissue of renal cell carcinoma. Membrane-bound neutral arylamidases from renal cell carcinoma, an intact part of the same kidney and placenta, had the same molecular weight (240 000) and were identical with respect to KM value and effect of inhibition by chelators or amino acids. Membrane-bound neutral arylamidase from renal carcinoma had the same electrophoretic mobility and heat stability as placental membrane-bound neutral arylamidase, but differed from kidney membrane-bound neutral arylamidase with respect to electrophoretic mobility, heat stability and susceptibility to urea inactivation. Results suggest the carcinoplacental alterations in membrane-bound neutral arylamidase isoenzyme in renal cell carcinoma.

Adenocarcinoma↗
PubMed1977

Comparison of human membrane-bound neutral arylamidases from small intestine, lung, kidney, liver and placenta.

Human membrane-bound neutral arylamidases were solubilized from small intestinal mucosa, lung, kidney, liver and placenta with trypsin. These five membrane-bound neutral arylamidases were identified by polyacrylamide gel-disc electrophoresis. The heat sensitivity of each enzyme was in the order, liver and placenta greater than kidney greater than lung greater than small intestine. This order correlates with that of electrophoretic mobility, except for the placental membrane-bound neutral arylamidase. Five membrane-bound neutral arylamidases have the same molecular weight, 240 000, as estimated by Sephadex G-200 gel filtration. The five membrane-bound neutral arylamidase have very similar KM values (8.7 x 10(-5) M towards L-alanyl-beta-naphthylamide), optimal pH values, hydrolysis ratios towards L-alanyl-beta-naphthylamide and L-leucyl-beta-naphthylamide, and sensitivities of inhibition by chelators or amino acids. These results suggest that the multiple forms of membrane-bound neutral arylamidase found in five different human organs are organ-specific isoenzymes.

Amino Acids↗
PubMed1977

Resistance mechanism of chloramphenicol in Streptococcus haemolyticus, Streptococcus pneumoniae and Streptococcus faecalis.

The chloramphenicol resistance of Streptococcus haemolyticus, Streptococcus pneumoniae and Streptococcus faecalis isolated from clinical materials was proved to be due to an inactivating enzyme produced by these bacteria. The inactivated products of chloramphenicol were identified as 1-acetoxy, 3-acetoxy and 1,3-diacetoxy derivatives by thin-layer chromatography and infrared spectroscopy. The responsible enzyme was thus confirmed to be chloramphenicol acetyltransferase. The enzyme was inducible. It was partially purified by ammonium sulfate precipitation, DEAE-cellulose chromatography and gel filtration on Sephadex G-150. The enzymes obtained from S. haemolyticus, S. pneumoniae and S. faecalis have been compared with the conclusion that they are identical with respect to molecular weight (approximately 75,000-80,000), optimum pH and heat stability.

Acetyltransferases↗
PubMed1976

[Bacteriological studies on doxycycline (Bonnamycin 'Cipan') (author's transl)].

Bonnamycin which is a new tetracycline group antibiotic isolated from a variant strain of Streptomyces rimosus and is identified chemically as doxycycline was investigated, comparing with tetracycline. The results are as follows: (1) In in vitro studies of anti-bacterial spectrum, doxycycline is widely effective against standard strains kept in our department. (2) The distribution of susceptibility of 75 Staphylococci, 62 Salmonella and 64 Shigella strains isolated from clinical materials was similar to that of tetracycline. (3) As to the therapeutic experiment in acute infection of Klebsiella pneumoniae in mice, the drugs were equally effective and the ED50 was both 70.8 mcg. (4) Doxycycline administrated orally or subcutaneously in rats was distributed in kidneys, livers, lungs and spleens at relatively high concentration among organs.

Acute Disease↗
PubMedDate not supplied

Expression of functional acetylcholine receptor from cloned cDNAs.

The cloned cDNAs encoding the four subunits of the Torpedo californica acetylcholine receptor, each carried by a simian virus 40 vector, direct the synthesis of the functional receptor in a combined expression system consisting of COS monkey cells and Xenopus oocytes. Our results suggest that all four subunits are required to elicit a normal nicotinic response to acetylcholine, whereas only the alpha-subunit is indispensable for alpha-bungarotoxin binding activity.

Animals↗
PubMedDate not supplied

Preventive effect of diethyldithiocarbamate on selenite-induced opacity in cultured rat lenses.

Increasing evidence suggests the involvement of reactive oxygen species in the development of cataracts. In this study, we investigated the preventive effect of diethyldithiocarbamate (DDC) on the selenite-induced opacification of cultured rat lenses. Lens opacity was produced by incubation with 0.2 mM selenite for 24 h, which resulted in an increase in selenium content in the cultured lenses. The increase in selenium content and the onset of opacification and lens membrane damage were inhibited by preincubation with DDC. It is reasonable to assume that DDC contributed to anticataract ability. In addition, selenite resulted in a significant decrease in glutathione and protein thiol content and an increase in lipid peroxidation levels in the lenses. These alterations were also depressed by DDC, suggesting a contribution of an antioxidative effect by DDC in the inhibition of lens opacification. At the same lens selenium content, DDC treatment inhibited opacification and lipid peroxide. In conclusion, we propose that the antioxidative properties of DDC play a major role in its contribution to the anticataract effect.

Adjuvants, Immunologic↗