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  • 1
    ISSN: 1432-1440
    Keywords: Polyacrylamide-gradient gels ; microelectrophoresis ; proteinuria ; glomerulonephritis ; Polyacrylamid-Gradientengele ; Mikroelektrophorese ; Proteinurie ; Glomerulonephritis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Es wird über die Anwendung der Mikroelektrophorese in Polyacrylamid-Gradientengelen zur Differenzierung der Proteinurie bei Glomerulonephritis berichtet. Die zeitlichen und methodischen Vorteile dieser Elektrophorese erlauben eine routinemäßige Durchführung in der Klinik. Durch die Auftrennung der Urinproteine nach ihrer Molekulargröße und Form lassen sich vier Proteinuriemuster unterscheiden: kleinmolekular, mittelmolekular, intermediär und hochmolekular. Glomerulonephritisformen, die konstante morphologische und klinische Veränderungen zeigen (z.B. minimal proliferierende Glomerulonephritis, mesangioproliferative Glomerulonephritis mit diffuser Halbmondbildung), lassen eine Zuordnung ihrer Proteinurie zu einem der vier Proteinuriemuster zu, während bei den anderen Glomerulonephritisformen (z.B. perimembranöse Glomerulone-phritis, mesangioproliferative Glomerulonephritis) eine Abhängigkeit des Proteinuriemusters von der Glomerulonephritisphase vermutet wird.
    Notes: Summary It is possible to differentiate the proteinuria of glomerulonephritis by means of microelectrophoresis in polyacrylamide-gradient gels. The advantages of this method (quick, cheap, concentration of the urine not required) led to its introduction into clinical use. Upon separating the urinary proteins according to their molecular weight and form, four patterns of proteinuria may be differentiated: low molecular, middle molecular, intermediate and high molecular. Those forms of glomerulonephritis which show constant morphological and clinical findings (e.g. minimal proliferative glomerulonephritis, mesangioproliferative glomerulonephritis with crescents) can be related to one of the four patterns of proteinuria, whereas the pattern of proteinuria in other forms of glomerulone-phritis (e.g. (peri-)membranous glomerulonephritis, mesangioproliferative glomerulonephritis) are dependent on the phase of the disease.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 57 (1979), S. 225-235 
    ISSN: 1432-1440
    Keywords: Angina pectoris ; Diagnostic criteria ; Myocardial infarction ; Serum myoglobin ; Radioimmunoassay ; Angina pectoris ; Diagnostik ; Myokardinfarkt ; Radioimmunoassay ; Serum-Myoglobin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Ein Radioimmunoassay zur Bestimmung von Serum-Myoglobin (SMb) wird vorgestellt. Bei 50 gesunden Probanden beträgt der Meßwertbereich 0–90 ng/ml. Serielle Bestimmungen an 10 Patienten mit akutem Myokardinfarkt beziehungsweise Angina pectoris (AP) zeigen, daß SMb bei Myokardinfarkt vor CK und CK-MB pathologische Werte erreicht (im Mittel 250±95 ng/ml bei stationärer Aufnahme 3,3±1,4 h nach AP-Beginn). Die gleichzeitig bestimmte NAC-aktivierte CK liegt zu diesem Zeitpunkt noch im Normbereich und erreicht pathologische Werte erst 6,2±1,9 h nach Schmerzbeginn. Der Peak des Serum-Myoglobins liegt mit 506±194 ng/ml 8,8±2,8 h, der der CK mit 905±475 mU/ml 20,0±7,8 h nach Anginabeginn. CK-MB und CK unterscheiden sich im zeitlichen Verlauf nur unwesentlich. Ein Patient mit ausgeprägter AP hat bei sonst unauffälligem Enzymmuster pathologisch erhöhte SMb-Werte. Methodische und klinische Ergebnisse werden diskutiert.
    Notes: Summary A radioimmunoassay was developed to determine serum myoglobin (SMb). 50 healthy persons showed values between 0 and 90 ng/ml. Serial tests of 10 patients following acute myocardial infarction or during angina pectoris (AP) indicated that SMb reached pathological values before CK and CK-MB (average 250±95 ng/ml at the time of hospitalisation which corresponds to 3.3±1.4 h after beginning of angina pectoris). At hospitalisation the simultaneously determined CK was within normal limits and reached pathological values only 6.2±1.9 h after the onset of angina. Maximum of SMb was 506±194 ng/ml occurring 8.8±2.8 h after the beginning of AP, maximum of CK was 905±475 mU/ml occurring 20.0±7.8 h after AP. CK-MB and CK differed only slightly in their time course. One patient with severe AP had pathologically increased SMb values whilst all other enzymes were completely normal. Methodical and clinical results are discussed.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0014-5793
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Naturwissenschaften 60 (1973), S. 476-476 
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1433-8580
    Keywords: Myelin basic protein ; Electrophoretic mobility test ; Gel electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Lymphocytes from seven patients with malignancies, from seven patients with non-malignancies, and from five healthy persons were incubated with125I-labeled MBP. Binding of MBP to lymphocytes was monitored from 0.5 to 20 h. The binding ranged from 4 to 7% of the total MBP present and remained fairly constant during the first 4 h of incubation. It dropped considerably at 20 h. Mean percentages of MBP binding were lower in cancer patients than in persons without malignancies. After incubation, the supernates were examined by gel electrophoresis. The electrophoretic pattern was similar in comparing groups with different diagnoses. A considerable loss of MBP in the terminal supernatant (20 h) was found. When tested in the electrophoretic mobility test (EM test) with stabilized erythrocytes, supernatant derived from cancer patients produced a somewhat higher mean slowing effect than did supernates from other patients and controls.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Entomologia experimentalis et applicata 19 (1976), S. 271-286 
    ISSN: 1570-7458
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Summary High numbers of simuliid bites may cause allergic reactions or even death in cattle due to the injection of salivary gland secretions. By means of micro-electrophoresis the proteins of the salivary glands and the hemolymph of three black fly species Boophthora erythrocephala, Odagmia ornata and Wilhelmia lineata were fractionated in polyacrylamide gel gradients in 10 μl capillaries. The molecular weight of the proteins was determined. The microtechnique applied allows a fractionation of salivary gland proteins from a single animal. Identical protein patterns mainly with relatively high molecular proteins (MW〉69000) were found in the spherical salivary glands in males and in the so-called accessory gland in females which has the same histological structure. The tube-shaped main gland which is only found in bloodsucking females contains several low molecular proteins (MW〉6000〈69000). These proteins are found neither in male nor in female hemolymph. These observations support the assumption that the females produce a specific type of salivary secretion in their main glands. During bloodsucking 50%–70% of the soluble salivary proteins are injected into the host animal. The recharging of the glands takes 4–5 hr. Proteins from the accessory glands show a very similar pattern to those of the hemolymph, but not to those in the main glands. This suggests a close relationship between the two sites. Membrane-bound proteins of the salivary glands can be fractionated as well on micro gel gradients after SDS charging. They differ from the water-soluble proteins. The ratio of these two types of proteins is 2:1. The proteins of a single salivary gland or parts of it can be fractionated without loss of material after complete solubilisation in SDS in a capillary directly on top of the separation gel.
    Notes: Zusammenfassung Kontinuierliche Gradienten-Gele in μl Kapillaren wurden zur Fraktionierung von wasserlöslichen und membranständigen Proteinen aus Speicheldrüsen und Hämolymphe von drei Simuliidenarten Boophthora erythrocephala (De Geer), Odagmia ornata (Meigen) und Wilhelmia lineata (Meigen) verwendet. Speicheldrüsen von Männchen und Weibchen haben jeweils charakteristische für die einzelne Art spezifische Bandenmuster. Das Proteinmuster der weiblichen Hauptdrüse unterscheidet sich deutlich von dem der Nebendrüse, das nahezu identisch ist mit dem Proteinmuster der männlichen Drüse. Die Hauptdrüse der Weibchen enthält im wesentlichen relativ neidermolekulare Proteine (〉6000〈69000); bei der Blutaufnahme werden 50%–60% von Haupt-und Nebendrüsenproteinen in das Wirtstier injiziert. Die Wiederauffüllung der Drüsen ist nach 4–5 Stunden abgeschlossen. Einige Proteine der Nebendrüse haben einen identischen Rf-Wert mit bestimmten Hämolymphproteinen. Dies spricht für eine Aufnahme von Hämolymphproteinen in die Drüse. Es wird gezeigt, daß eine einzelne Drüse mit einem Proteingehalt von ca. 3 μg für eine Fraktionierung ausreicht, wenn die Drüse direkt über dem Gel mit SDS inkubiert wird.
    Type of Medium: Electronic Resource
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