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Biomedical subjects

M Dürr

Publications and source records attributed to M Dürr.

34 records · Page 2Linked to original sources
PubMed1999

A voice-controlled robotic assistant for neuroendoscopy.

This paper describes experiments with a voice-controlled robot system to be used in endoscopic neurosurgery. The robot was a modified version of the robot described in previous publications of the group at Fraunhofer IPA and HSK. To control the robot a voice-controlled user interface was developed. The experiments were conducted on cadavers for three standard approaches in neuroendoscopy. The goal was to gain experience with a voice-controlled user interface and also with the set-up and use of the robotic system under clinical conditions. The results indicate that modifications to the robot and user interface are necessary. However the overall feasibility of the application was demonstrated.

Endoscopy↗
PubMed1992

Integration of radiology and hospital information systems (RIS, HIS) with PACS: requirements of the radiologist.

PACS development has now reached a stage where it can clearly be stated that the technology for storage, networking and display in a fully digital environment is available. This is reflected by an already large and rapidly increasing number of PACS installations in USA, Western Europe and Japan. Such installations consist of a great variety of information systems, more or less interconnected, like PACS, HIS, RIS and other departmental systems, differing in both hardware and software. Various data - even if they only concern one person - are stored in different systems distributed in the hospital. The integration of all digital systems into a functional unit is determined by the radiologist's need of quick access to all relevant information regardless where it is stored. The interconnection and functional integration of all digital systems in the hospital determine the clinical benefits of PACS. This paper (1) describes the radiologist's requirements concerning this integration, and (2) presents some realistic solutions such as the Siemens ISI (Information System Interface), and a mobile viewing station for the wards (visitBox).

Austria↗
PubMed1992

Measurement of particle and mass distribution of pentamidine aerosol by ultrasonic and air jet nebulizers.

The use of appropriate nebulizers is a major precondition for a successful treatment and prevention of Pneumocystis carinii pneumonia with pentamidine aerosol. The apparatus should supply a sufficient amount of pentamidine with adequate particle size. Using Fisons ultrasonic nebulizer FISO Neb, model FZV 40 BAMKI, De Vilbiss ultrasonic nebulizer, Porta-Sonic, model 8500 GB, and the Marquest Medical Products jet nebulizer Respirgard II, two pentamidine concentrations (300 mg/6 ml and 60 mg/6 ml) were compared by measuring nebulized pentamidine mass distribution and particle size distribution under in vitro conditions by means of a laser light-scattering particle sizer of the type Malvern Master sizer. It was found that there were significant differences among nebulizers. Mass distribution experiments with air flow 6 l/min showed that using FISO Neb the quantity of nebulized pentamidine was 201.4 mg and 36.7 mg, whereas using Porta-Sonic the values found decreased to 85.2 mg and 23.6 mg. Using Respirgard II the values were 80.0 mg and 10.64 mg. The measured total duration times of nebulization were 6 - 8.5 min, 12 min and 25 min for the nebulizers FISO Neb, Porta-Sonic and Respirgard II. A decomposition of pentamidine during nebulization in the case of ultrasonic nebulizers doesn't take place. The measured mass median diameters (MMD) were 5.6 - 6.9 mum, 1.96 - 3.04 mum and 1.9 - 2.5 mum for the nebulizers FISO Neb, Porta-Sonic and Respirgard II. Using 300 mg pentamidine the nebulized amounts of pentamidine containing particles sizes less than or equal to 2 mum predominately available for alveolar deposition were with values of about 43 mg markedly higher for Respirgard II and Porta-Sonic than the measured 10.5 mg for FISO Neb.

Aerosols↗
PubMed1980

Involvement of Lipid-linked Oligosaccharides in Synthesis of Storage Glycoproteins in Soybean Seeds.

Membrane preparations from developing soybean (var. Prize) cotyledon tissue, at the time of synthesis of storage glycoproteins, catalyze the sequential assembly of lipid-linked oligosaccharides from uridine-5'-diphospho-N-acetyl-d-[6-(3)H] glucosamine and guanosine-5'diphospho-d-[U-(14)C]mannose. The maximum size of lipid-linked oligosaccharide that accumulates contains the equivalent of 10 saccharide units on the basis of Bio-Gel P-2 gel filtration studies. These lipid-linked oligosaccharides show similar characteristics to polyisoprenyl diphosphate derivatives on diethylaminoethyl-cellulose chromatography and are potential intermediates in glycoprotein biosynthesis in this tissue. These glycolipids do not appear to turn over in pulse-chase experiments and no completed storage glycoproteins were detected among the products of these incubations.Tissue slices from cotyledons at the same stage of development synthesize lipid-linked oligosaccharides from [(3)H]mannose and [(3)H]glucosamine with sizes equivalent to 1, 7, 10, and approximately 15 saccharide units. In pulse-chase experiments, the lipid-linked saccharides with the equivalent of 1 and 10 units rapidly turnover, whereas those with 7 and 15 units do not. Examination of the higher oligosaccharide peaks (10 and 15) by Bio-Gel P-4 gel filtration shows them to comprise 2 distinct subsets of oligosaccharides containing different proportions of glucosamine and mannose units. Tissue slices synthesize products which resemble the completed 7S storage glycoproteins as judged by similarity of molecular weight and precipitation with specific antisera. Analysis of the oligosaccharides obtained by hydrazinolysis of glycoproteins shows the presence of a similar size "high-mannose" type N-linked oligosaccharides as in other glycoproteins from animal and plant cells.

Journal Article↗
PubMed1979

The assembly of lipid-linked oligosaccharides in plant and animal membranes.

Membrane preparations from growing regions of pea stems and actively-dividing mouse L-cells form lipid-linked saccharides from GDP-mannose and UDP-N-acetylglucosamine. These lipids have properties which are consistent with those of mono- and di-phosphoryl polyisoprenyl derivatives. In experiments using plant membranes, the monophosphoryl derivative labeled with GDP-(14C) mannose contains mannose only, while the diphosphoryl derivative labeled with the same nucleotide sugar is heterogeneous, containing oligosaccharides corresponding to mannosaccharides of 5, 7, and 9--12 residues. Only the diphosphoryl polyisoprenyl derivatives are labeled with UDP-(14C)glucosamine and these contain predominantly chitobiose and N-acetylglucosamine itself. Unlabeled GDP-mannose added after UDP-N-acetyl-(14C)glucosamine results in the formation of higher lipid-linked oligosaccharides which are apparently the same as those which are labeled with GDP-(14C)mannose alone. Incubation of the membranes with GDP-(14C)mannose in the presence of Mn2+, unlabeled UDP-glucose or unlabeled UDP-N-acetylglucosamine results in marked changes in the accumulation of both the polyisoprenyl monophosphoryl mannose and polyisoprenyl diphosphoryl oligosaccharides. Animal cell membranes synthesise lipid-linked oligosaccharides when incubated with UDP-N-acetylglucosamine and GDP-mannose. These oligosaccharides are similar in size to those synthesised by the plant membranes but their formation is more efficient. The potential roles of these compounds in glycoprotein biosynthesis in both plant and animal tissues is discussed.

Glycoproteins↗
PubMed1978

Localization of polyphosphate in vacuoles of Saccharomyces cerevisiae.

Virtually all of the polyphosphate (PP) present in yeast protoplasts can be recovered in a crude particulate fraction if polybase-induced lysis is used for disrupting the protoplasts. This fraction contains most of the vacuoles, mitochondria and nuclei. Upon the purification of vacuoles the PP is enriched to the same extent as are the vacuolar markers. The amount of PP per vacuole is comparable to the amount of PP per protoplast. The possibility that PP is located in the cell wall is also considered. In the course of the incubation necessary for preparing protoplasts, 20% of the cellular PP is broken down. As this loss of PP occurs to the same extent in the absence of cell wall degrading enzymes, it is inferred that internal PP is metabolically degraded, no PP being located in the cell walls. It is concluded that in Saccharomyces cerevisiae most if not all of the PP is located in the vacuoles, at least under the growth conditions used.

Cell Wall↗
PubMed1976

Asymmetric distribution of concanavalin A binding sites on yeast plasmalemma and vacuolar membrane.

Isolated vacuoles of Saccharomyces cerevisiae did not bind Concanavalin A (labelled with tritium or with a fluorescent dye) unless the vacuoles were rendered permeable and their inner membrane surface made accessible. Yeast protoplasts, on the other hand, bound large amounts of Concanavalin A on their surface, and the number of binding sites was not increased after a gentle lysis expected to expose also the inner surface of the plasmalemma. It is concluded that both the plasmalemma and the vacuolar membrane carry Concanavalin A binding sites exclusively on the surface opposite to the cytoplasmic matrix.

Binding Sites, Antibody↗
PubMed1975

Polybase induced lysis of yeast spheroplasts. A new gentle method for preparation of vacuoles.

The polybasic macromolecules DEAE-dextran (diethylaminoethyl-dextran, molecular weight 500000) and poly-DL-lysine (molecular weight 30000-70000) were absorbed with a high affinity by spheroplasts of Candida utilis and subsequently, induced lysis. The extent of lysis of spheroplasts and of the liberated vacuoles was studied under various conditions using alpha-glucosidase activity and soluble arginine as cytoplasmic and vacuolar markers, respectively. Adsorption of polybases was rapidly completed even at 0 degrees C; however, with small doses, lysis was poor at 0-12 degrees C and extensive at temperatures above 12 degrees C. This permitted the completion of adsorption before initiating lysis. The purified vacuoles were also sensitive to polybases though less so than the spheroplasts; however, after lysis of spheroplasts the liberated vacuoles were well protected against the action of polybases. A treatment with polybases which disrupted more than 99% of the spheroplasts left at least 70% of the vacuoles intact. Potassium chloride in high concentrations and calcium chloride in low concentrations inhibited polybase induced lysis of spheroplasts by preventing or even reversing the polybase adsorption. A polyacidic macromolecule, dextran sulfate, could prevent but not reverse the adsorption of polybase and subsequent lysis. Metabolic inhibitors reduced the susceptibility of spheroplasts to polybase induced lysis. Vacuoles isolated from polybase lysed spheroplasts still contained large pools of soluble amino acids, and their ability to transport arginine specifically is a further indication of their functional integrity.

Arginine↗
PubMed1975

Characterization of a specific transport system for arginine in isolated yeast vacuoles.

The transport of L-arginine was studied in isolated vacuoles of Saccharomyces cerevisiae. A centrifugation method allowed rapid separation of the fragile vacuoles from the incubation media so that initial uptake rates of [14C]arginine could be measured. Labelled arginine added to the medium was accumulated in the isolated vacuoles; it was found to exchange specifically with the arginine already present in the vacuoles. Such an exchange did not take place in intact spheroplasts. The pH dependence of the arginine transport in the vacuoles was tested. As the vacuoles are unstable in the pH range of optimal transport activity (pH above 7.0), the pH optimum of the transport reaction could not be determined. From the temperature dependence, the apparent energy of activation was calculated to be 9800 cal/mol. Arginine transport shows saturation kinetics with an apparent Km of 30 muM in the isolated vacuoles, and of 1.5 muM in the spheroplasts. Competition experiments with amino acids and arginine analogues demonstrated that the arginine transport in both vacuoles and spheroplasts, is highly specific. The two systems, however, were shown to have distinct specificities. The inhibition of vacuolar L-arginine transport by D-arginine, L-histidine, and L-canavanine was competitive with apparent Ki values of 60 muM, 400 muM and 600 muM respectively.

Amino Acids↗