Publications by authors named "Adelmann B"

We report on additively manufactured filter systems based on bionic manta ray structures and evaluate their filter performance. The filters are periodic lamella structures produced by selective laser sintering using PA12 polyamide powder. Two different lamella types are investigated, which are derived from two manta ray genera, namely, and .

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We present a compressed air motor, completely built by laser powder bed fusion. To highlight the fully functional integration by additive manufacturing, the rotor, stator, bearings, turbine, gas inlet and outlet were all built in a single print job. The material used was Inconel 718, and the motor was 44 mm tall and 12 mm in diameter.

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We present an in situ process monitoring approach for remote fiber laser cutting, which is based on evaluating images from a high-speed camera. A specifically designed image processing algorithm allows the distinction between complete and incomplete cuts by analyzing spectral and geometric information of the melt pool from the captured images of the high-speed camera. The camera-based monitoring system itself is fit to a conventional laser deflection unit for use with high-power fiber lasers, with the optical detection path being coaxially aligned to the incident laser.

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In this contribution, we compare basic neural networks with convolutional neural networks for cut failure classification during fiber laser cutting. The experiments are performed by cutting thin electrical sheets with a 500 W single-mode fiber laser while taking coaxial camera images for the classification. The quality is grouped in the categories good cut, cuts with burr formation and cut interruptions.

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In this publication, we use a small convolutional neural network to detect cut interruptions during laser cutting from single images of a high-speed camera. A camera takes images without additional illumination at a resolution of 32 × 64 pixels from cutting steel sheets of varying thicknesses with different laser parameter combinations and classifies them into cuts and cut interruptions. After a short learning period of five epochs on a certain sheet thickness, the images are classified with a low error rate of 0.

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We report on a photodiode-based sensor system to detect cutting interruptions during laser cutting with a fiber laser. An InGaAs diode records the thermal radiation from the process zone with a ring mirror and optical filter arrangement mounted between a collimation unit and a cutting head. The photodiode current is digitalized with a sample rate of 20 kHz and filtered with a Chebyshev Type I filter.

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We have identified and characterized insulin-like growth factor I (IGF-I) and IGF-II/mannose-6-phosphate (IGF-II/M6P) receptors in bovine adrenal cells. Iodine-125-labeled IGF-I ([125I]IGF-I) binding was characteristic of the IGF-I receptor, and binding kinetics as well as receptor densities were similar in cortical and medullary membranes. Scatchard analysis of [125I]IGF-I binding to cultured adrenocortical cells showed a single class of high-affinity binding sites with a Kd of 1.

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The narcotic agent etomidate and the antimycotic drug ketoconazole are known to block steroid biosynthesis in man. To study the different effects of these imidazole derivatives on human adrenal steroid biosynthesis we incubated slices of human adrenal glands with 3H-labeled precursors and increasing concentrations of etomidate or ketoconazole (0-2000 microM). After extraction the labeled metabolites were separated by thin-layer chromatography and quantified by scintillation counting.

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Ketoconazole, an imidazole antimycotic drug, inhibits steroid biosynthesis in adrenal and testicular tissue by blocking cytochrome P-450 dependent enzymes. To study the effect of ketoconazole on steroid biosynthesis in the human ovary we incubated human ovarian tissue (mainly theca cells) or granulosa cells with radiolabeled precursors and increasing concentrations of ketoconazole. After incubation, steroids were extracted and separated by thin layer chromatography (TLC).

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Native and denatured 125-I-collagen were reacted with sera from 366 patients undergoing orthopedic surgery. Complexes consisting of native or denatured collagen and immunoglobulins or of denatured collagen and cold insoluble globulin were precipitated with secondary antibodies to either immunoglobulins or CIG. Only approximately 10% of the patients' sera bound more than 5 ng native collagen/10 microliter serum.

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Antigelatin factor, a protein capable of complexing denatured collagen, was separated from human serum by adsorption onto immobilized collagen. Antiserum raised against the material binding to denatured collagen permitted the development of a radioassay for the determination of antigelatin factor in which the complex of antigelatin factor and denatured 125I-labeled collagen is precipitated with this antiserum. Further purification of antigelatin factor was achieved by chromatography on DEAE-cellulose yielding an electrophoretically homogeneous protein.

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A protein known as antigelatin factor (AGF) was isolated from human serum by affinity chromatography with immobilized denatured collagen. In biochemical and immunological assays AGF showed specificity to denatured, but not to native collagen of the types I, II and III. A close relationship to Cell Attachment Protein and Cold Insoluble Globulin was found in comparative studies.

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Anti-gelatin factor was prepared from guinea-pig and human serum by affinity chromatography on denatured type-I collagen. As shown previously, this component is related to cold-insoluble globulin. It reacted with 125I-labelled denatured collagen, and the reaction could be inhibited by preincubation with unlabelled collagenous components.

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The immunological response to collagen of guinea-pigs is strongly dependent on the conformation of the antigen and on the type of adjuvant. Freund's complete adjuvant facilitated excellent delayed hypersensitivity skin reactions to native (triple helical conformation) as well as denatured (random coil conformation) collagen. Immunization of guinea-pigs with collagen in this adjuvant gave rise to very low levels of antibody to native collagen and failed to induce antibodies to denatured collagen.

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Cutaneous delayed hypersensitivity reactions to collagen in guinea-pigs were partially but specifically suppressed if the animals had been pretreated with collagen and Freund's incomplete adjuvant. Such animals responded normally to skin-reactive factor prepared with ovalbumin. Lymphoid cells from animals with normal delayed hypersensitivity to collagen functioned normally in animals with suppressed skin reactivity.

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Partial suppression of cutaneous delayed hypersensitivity reactions to collagen in guinea-pigs was induced by pre-immunization with collagen and FIA. This suppression is specific since: (a) pretreatment with OA and FIA or FIA alone did not cause suppression of skin reactions to collagen; (b) suppression was observed only if the collagen used for pretreatment was from the same species as that employed for sensitization for delayed hypersensitivity reactions; and (c) animals with depressed skin reactivity to collagen reacted normally to PPD. The suppression is not mediated by inducible, circulating antibodies to collagen since: (a) antibody titres measured by passive haemagglutination did not correlate with the degree of suppression; (b) suppression was observed with collagen in random coil conformation which sensitizes guinea-pigs for delayed hypersensitivity skin reaction but does not induce antibodies to denatured collagen; (c) best suppression was obtained if the animals were pretreated with collagen and FIA 3 days before the sensitizing injection; and (d) passively transferred antibody from animals with suppressed skin reactivity did not suppress skin reactivity of animals made hypersensitive to collagen by injection of collagen and FCA.

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Guinea-pig peritoneal exudate cells were tested in vitro in the presence or absence of specific antiserum to native collagen for their capacity to discriminate between native and denatured collagens of various species. Adherent exudate cells bound denatured collagens, regardless of the origin of the collagen or the presence of serum. The binding was reduced if the cells were pretreated with trypsin.

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Sections of arterial walls and of thrombi and smears of leukocytes previously incubated in vitro with collagen type III were examined by immunohistochemical technique for the presence of collagen types I, II and III. In arterial walls collagen type III was detected immediately underlaying the endothelial cell layer and in the tissue between tunica elastica interna and adventitia. Collagen type I was not shown in the subendothelial layer.

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