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Biomedical subjects

M Ueda

Publications and source records attributed to M Ueda.

At least 1,369 records · Page 76Linked to original sources
PubMed1983

[The effect of prostaglandin F2 alpha on the gastrointestinal movement after urological surgery].

To facilitate postoperative flatus, Prostaglandin F2 alpha (PGF2 alpha) was given intravenously to 23 patients who underwent urological operations. The patients were 14 males and 6 females aged from 20 to 77 years old. Patients with hypertension or cardiovascular disease were not included. Twelve operations were performed under general anesthesia, and 8 under epidural anesthesia. Thirteen operations were performed for the upper urinary tract or adrenal gland, and 5 were for the lower urinary tract. In 2 cases, the peritoneal cavity was opened and operations were performed on the intestines. PGF2 alpha 2000 micrograms was added to the postoperative drip infusion and administered in 2 to 3 hours. Until the first flatus was recognized, PGF2 alpha was given once a day in the same manner. Twenty-six patients, 10 of whom were given either vagostigmine or pantothen postoperatively, served as the control group. PGF2 alpha accelerated the postoperative flatus by 8.7 hours (mean) compared with the control group, but it was not significant. The onset of flatus was significantly promoted under epidural anesthesia. Gastrointestinal movement tended to be facilitated in the PGF2 alpha group after lower urinary tract surgery and in the patients over 50 years old. Three patients complained of severe abdominal pain as a side effect; and, injection of PGF2 alpha was stopped. In 7 patients, mild stomachache , vascular pain, nausea, vomiting or elevation of blood pressure were observed.

Adult↗
PubMed1982

The subcomponent Clq of the first component of guinea pig complement: purification and characterization.

Guinea pig C1q was purified, in a highly active hemolytic form, by a combination of precipitation with chelating agents, CM-cellulose and Sepharose 6B. Yields ranged from 30 to 35% protein, and the activity of final preparations was in the range of 2 x 10(13)--3 x 10(13) C1q effective molecules/mg. The molecular weight of C1q was approximately 430,000, as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS). C1q was shown to be composed of two non-covalently liked subunits of approximate molecular weights 46,500 and 45,000 in a molar ratio 2:1. One reduction, the higher molecular weight subunit gave two chains having approximate molecular weights of 24,500 and 23,000 in equimolar ration, and the lower weight subunit gave one chain with a molecular weight of approximately 22,300. C1q contained hydroxyproline, hydroxylysine and high percentage of glycine. Thus, the overall molecular structure of guinea pig C1q appears similar to that of human C1q. The antiserum against the purified C1q showed only one precipitation band with guinea pig whole serum or purified C1q on immunodiffusion analyses and was found to be monospecific.

Amino Acids↗
PubMed1982

Revascularization of autogenous skin grafts placed on irradiated tissue.

Vascular changes in rat skin after irradiation were examined microangiographically. Revascularization of the skin transplanted during the chronic stage after irradiation was also studied. The results obtained through these examinations revealed higher vascular densities at the acute and the subacute stages, and low values at the chronic stages compared with those of the control. Furthermore, when the skin grafts were transplanted to the irradiated beds in the chronic stage, primary revascularization was scant, and the inhibited capillary proliferation in the recipient sites prevented new vessel penetration. This explains to why grafts transplanted to previously irradiated beds fail to survive.

Angiography↗
PubMed1982

Peroxisomal and mitochondrial carnitine acetyltransferases in alkane-grown yeast Candida tropicalis.

Two types of carnitine acetyltransferases (EC 2.3.1.7) were first isolated from a microorganism, alkane-grown yeast Candida tropicalis. Carnitine acetyltransferase activity was induced in the alkane-grown cells, reaching about twenty times higher than that in the glucose-grown cells. Localization of the enzyme activity was demonstrated, at least, in peroxisomes (microbodies), profusely occurred in the alkane-grown cells, and in mitochondria. Peroxisomal and mitochondrial carnitine acetyltransferases could be separated using the method of DEAE-Sephacel column chromatography and both types were found to exist in the alkane-grown cells of C. tropicalis. Each carnitine acetyltransferase was purified using Sephadex G-200, Sepharose 6B, DEAE-Sephacel and Blue-Sepharose CL-6B. In DEAE-Sephacel chromatography, peroxisomal carnitine acetyltransferase was eluted below 0.15 M KCl concentration and mitochondrial carnitine acetyltransferase above 0.15 M KCl concentration. Except for the localization, little difference was observed in their kinetic properties, substrate specificity and so on. These two carnitine acetyltransferase preparations were only specific to acetyl and propionyl groups, the substrate specificity not being so broad as that of carnitine acetyltransferase obtained from mammalian tissues. Roles of these carnitine acetyltransferases in alkane metabolism in yeast are also discussed.

Acetyltransferases↗