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Biomedical subjects

K Ohno

Publications and source records attributed to K Ohno.

At least 793 records · Page 44Linked to original sources
PubMed1976

[The fecal flora of man. IV. Communication: Comparison of the newly developed method with the old conventional method for the analysis of intestinal flora (author's transl)].

The results of 42 fecal flora analysis of healthy adult men were compared by using a newly developed method and an old conventional method. Statistical estimate indicate, that with the new method the total counts and the counts of bifidobacteria, catenabacteria (eubacteria and anaerobic lactobacilli), peptostreptococci, and clostridia (except Cl. perfringens) as well as the occurences of peptostreptococci and spirillaceae were significant higher than with the use of the old method. On the other hand the counts and occurences of bifidobacteria, veillonellae, Cl. perfringens, Megasphaerae and aerobes were similar with both method. With the new method the total counts of feces of healthy adult men nubmered 1-2 X 10(11) per g wet weight, and fastidious anaerobes, such as bacteroides, catenabacteria and peptostreptococci, were always occurred as predominant flora. The results suggest that the conventional anaerobic jar method is inadequate for the isolation of fastidiuos anaerobes and indicate that the use of modified medium 10 in combination with strict anaerobic technique is necessary for the analysis of fecal flora.

Adult↗
PubMed1975

Partial purification and properties of phospholipase A2 from the starfish, Asterina pectinifera.

1. Phospholipase A2 (phosphatide 2-acyl-hydrolase, EC 3.1.1.4) activity was shown to occur in the supernatant fraction of a freshly prepared homogenate from the pyloric caecum of starfish (Asterina pectinifera). 2. The phospholipase A2 has been isolated and purified 130-fold by ultracentrifugation, ammonium sulfate precipitation and column chromatographic procedures. 3. The purified enzyme was stable to heat at low pH values and the optimal pH was observed at approximately 9.0. 4. The enzyme activity was activated by Ca2+ and sodium deoxycholate, and was inhibited by EDTA.

Animals↗
PubMed1975

Acyltransferase activities in rat lung microsomes.

Some properties of acyl-CoA:1-acyl-sn-glycero-3-phosphorylcholine acyl-transferase in rat lung microsomes wed moiety of acyl-CoAs, quite different values were obtained on the Michaelis constant, the maximal velocity, and the activation energy. Moreover, the incorporation of fatty acid from an acyl-CoA was affected in a different manner by the addition of other acyl-CoAs. These results suggested that there are at least two different acyltransferases which are tentatively termed as follows: (1) palmitoyl-CoA: 1-acylglycerophosphorylcholine acyltransferase; and (2) arachidonoyl-CoA: 1-acylglycerophosphorylcholine acyltransferase. A low Km value, a low maximal velocity, and a low value of the activation energy were obtained for the former activity. The activity is readily inhibited by the addition of other acyl-CoAs and also at the higher concentration of palmitoyl-CoA itself. While a high Km value, a high maximal velocity, and a high value of the activation energy were obtained for the latter activity. The activity is not affected by the addition of palmitoyl-CoA or oleoyl-CoA and only slightly inhibited by linoleoyl-CoA, which indicates a high substrate specificity for polyenoyl-CoA especially for arachidonoyl-CoA. It seems that the present result, together with the previous findings obtained in slice experiments and in in vivo studies, do not support the idea that palmitoyl-CoA : 1-acylglycerophosphorylcholine acyltransferase participates in the main pathway for the formation of dipalmitoyllecithin in lung.

Acyltransferases↗
PubMed1975

Substrate-selectivity of rat liver microsomal 1,2-diacylglycerol: CDP-choline(ethanolamine) choline(ethanolamine)phosphotransferase in utilizing endogenous substrates.

Rat liver microsomes containing 1,2-diacylglycerols formed from the endogenous phosphatidycholines by the action of 1,2-diacylglycerol: CDPcholine cholinephosphotransferase (E.C. 2.7.8.2.) were used as a source of enzymes and substrates. A marked selectivity of 1,2-diacylglycerol: CDPethanolamine ethanolaminephosphotransferase (E.C. 2.7.8.1.) was revealed for utilizing endogenous hexaenoic diaglycerol, while cholinephosphotransferase utilized without marked selectivity the endogenous 1,2-diacylglycerol species differing in the degree of unsaturation. By using microsomes prepared after injecting the animals with 1-acyl lysophosphatidylcholines labeled with radioactive myristic, palmitic, and stearic acids, the selectivity of the transferases towards the saturated fatty acids in the 1-position of the endogenous substrates was studied. In incubation of the labeled microsomes with CMP, cholinephosphotransferase appeared to utilize 1-myristyl phosphatidylcholine most rapidly and, in decreasing order, the 1-palmityl and 1-stearyl species. Ethanolaminephosphotransferase utilized the endogenous 1-stearyl diacylglycerol in preference to 1-palmityl type.

Animals↗