[Nosocomial infections in gynecology and obstetrics (proceedings)].
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Biomedical subjects
Publications and source records attributed to K Decker.
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During recent years, catheter angiography of the cerebral vessels has tended to displace direct puncture of the carotid arteries. The method has significant advantages for the radiologist and the patient. A number of procedures are described which make this examination more easily performed, increase its diagnostic value and, most important, render it safer for the patient. Changes in catheter technique, in the radiographic apparatus and in the scope of the method are discussed.
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A total of 2,357 sterilizations via bipolar coagulation was effected at the University Clinics of Gynecology at Basel and Tübingen since 1972 and 1975 respectively. Of these, 2,143 were effected via laparoscopy. The following complications occurred which required laparotomy: in two cases, hemorrhages from the abdominal cavity as a result of the second puncture, in one case from the mesosalpinx, and, as a late complication, two extrauterine pregnancies. The method failed in the case of the two extrauterine pregnancies and possibly also in the case of two doubtful intrauterine pregnancies (0.8--1.7 per thousand). Today this surgical measure is being performed in Tübingen exclusively by the single-puncture technique an increasingly under local anesthesia. The advantages of the method are an accurately determinable coagulation zone, sparing of the mesosalpinx, low incidence of complications, absence of life-threatening incidents, and low failure quota.
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Resting cell suspensions of Arthrobacter oxidans were shown to synthesize the inducible enantiozyme, D-6-hydroxynicotine oxidase, in the presence of D-nicotine or D-6-hydroxynicotine. The corresponding L-enantiomers, as well as gamma-methylaminopropyl-(6-OH-pyridyl-3)-ketone, which is the product of the reaction catalyzed by the enzyme, were ineffective as inducers. L-6-Hydroxynicotine inhibited induction by D-nicotine and D-6-hydroxynicotine while L-nicotine inhibited induction by D-6-hydroxynicotine and had no effect on induction by D-nicotine. Enzyme induction was also found to be inhibited by glucose, 2-deoxy-D-glucose and by several intermediates of the tricarboxylic acid cycle. An absolute requirement for protein synthesis and for oxygen was also demonstrated to be necessary for the reactions involved in the covalent attachment of flavin adenine dinucleotide to pre-existing precursor protein to yield the catalytically active D-6-hydroxynicotine oxidase.
D-Galactosamine reduces the hepatic content of uridine phosphates, UDP-galactose, and UDPglucose due to an accumulation of UDP-amino sugars; this deficiency can result in severe hepatocellular damage. Alterations of glycosphingolipid synthesis in the early phase of this pathogenic process were studied by measurements of the incorporation of labeled galactose into glycosphingolipids of rat liver. [1-14C]Galactose was injected 2 h after galactosamine administration and the specific radioactivities of the glycosphingolipid precursors, UCPgalactose and UDPglucose, were determined. The specific radioactivity of UDPgalactose, when integrated over the whole period of radioactive synthesis, was four times higher in the galactosamine-treated animals than in the controls; the corresponding ratio of UDPglucose was 0.85. The pattern of the glycosphingolipids isolated from the livers of normal and galactosamine-treated rats resembled that described by Siddiqui and Hakomori (1970, Cancer Res. 30, 2930-2936); GL1, GM3,GM1, GD1, and a small amount of GT could be characterized. The specific radioactivities of glucose and galactose obtained from individual glycosphingolipids were determined in normal and galactosamine-treated livers. The synthesis of the glycosphingolipids was calculated using the respective data of the UDPhexoses. The labeling of glucosylceramide (GL1) was not altered and only a small change of GM3 could be detected; the synthesis of gangliosides GM1 and GD1, however, was inhibited by 95% or more between 4 and 6 h after galactosamine administration.
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Enzymic iodination of isolated rat hepatocytes and of rat livers perfused in situ was used to discriminate between the nucleotide pyrophosphatases of endoplasmic reticulum and of plasma membranes. The location of the latter on the cell surface could also be substantiated by this method. The activity of the microsomal enzyme increased after phenobarbital treatment of the animals. The nucleotide pyrophosphates from both subcellular fractions were solubilized, purified to electrophoretic homogeneity, and their 125I content determined. The labelling of the enzyme obtained from plasma membranes was several-fold higher than that of the nucleotide pyrophosphatase from endoplasmic reticulum. This indicates a bimodal distribution of nucleotide pyrophosphatase in rat liver and the accessibility of the plasma membrane enzyme from the extracellular space.
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A new film changer is described which permits serial films to be obtained, it can be used without attenuation of radiation to the image intensifier. Details of the serial changer, such as speed and resolution are described.
Isolated rat hepatocytes preserved for several hours their contents of ATP, CTP, GTP, UTP and UDPG. Leakage of intracellular and membrane-bound enzymes remained in the range observed with the isolated perfused rat liver. D-Galactosamine led to a rapid decrease of the UTP and UDPG contents while ATP and GTP levels remained unaffected. The sum of acid-soluble uracil nucleotides increased immediately after the addition of D-galactosamine, indicating release of the UTP-mediated feed-back inhibition of pyrimidine nucleotide de novo biosynthesis. Addition of uridine to a hepatocyte suspension resulted in a rapid increase in the levels of uridylate derivatives; the concentrations of UTP and UDPG, previously depleted by D-galactosamine, were restored within 1 h. Isolated hepatocytes appear suitable for studies on the pathogenic sequence of events elicited by D-galactosamine and on the regulation of pyrimidine biosynthesis.
The nucleoti-e contents of isolated rat Kupffer cells were found to be smaller than those of hepatocytes. The rate of UDPGal formation from D-galactose was much lower in Kupffer cells than in hepatocytes. The viability of the former was checked by measuring the leakage of enzymes and the formation of UTP from uridine. Addition of GalN to isolated Kupffer cells did not decrease their UTP and UDPG contents as much as those of hepatocytes. The same results were obtained when cells were isolated from GalN-pretreated animals. The incorporation of labeled amino acids into protein after GalN addition was much less reduced in Kupffer cells than in hepatocytes. The data suggest that Kupffer cells do not contribute to GalN-induced liver injury as a result of uridylate trapping.
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