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  • 1
    Electronic Resource
    Electronic Resource
    Über eine neue erythrocytäre Glucose-6-Phosphatdehydrogenase-Variante, ‚Typ Frankfurt‘ (1974)
    Springer
    Journal of molecular medicine 52 (1974), S. 478-484 
    Details
    ISSN: 1432-1440
    Keywords: New erythrocyte G-6-PD variant ; kinetical parameters ; Neue erythrocytäre G-6-PD-Variante ; Enzymkinetische Parameter
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Es wird über Untersuchungen zur Charakterisierung einer neuen erythrocytären G-6-PD-Variante, die in einer deutschen Sippe gefunden wurde, berichtet. Nachdem bereits vorausgegangene Familienuntersuchungen den allosomalen an das X-Chromosom gebundenen Erbgang aufgezeigt hatten, wurde jetzt aus den Erythrocyten eines hemizygoten Erbmalsträgers dieser Sippe das Enzym teilweise gereinigt und angereichert; in dieser Enzymanreicherung wurden die Aktivität, die elektrophoretische Wanderungsgeschwindigkeit, die Michaeliskonstante für G-6-P und NADP, die relative Utilisationsrate von 2-d-G-6-P und Gal-6-P, die Thermostabilität, die Aktivierung durch Hitze und die pH-Optima untersucht. Der Vergleich dieser Untersuchungsergebnisse mit den aus der Literatur bekannten Werten von 117 weiteren G-6-PD-Varianten und mit den eigenen Ergebnissen von parallel-laufenden Untersuchungen am normalen Enzymtyp Gd B zeigte, daß es sich bei dem untersuchten Enzym um eine neue Variante handelt, die den Empfehlungen der WHO entsprechend als Typ Frankfurt bezeichnet worden ist.
    Notes: Summary The paper reports on the results of investigations on the characterization of a new erythrocyte G-6-PD variant, which was found in a German family. Earlier family investigations had already revealed an allosomal X-chromosome linked heredity. The enzyme was isolated and purified from erythrocytes of a hemizygous carrier of the enzyme defect. This enzyme preparation was used for the determination of the following parameters: enzyme activity, electrophoretic mobility, Michaelis constants for glucose-6-phosphate and NADP, relative rate of utilisation for 2-deoxyglucose-6-phosphate and galactose-6-phosphate, thermostability, thermo-activation, and pH-optima. The results were compared with the known data of 117 other G-6-PD variants and with own results of parallel studies on the normal enzyme Gd B. The enzyme in question could be shown to represent a new variant. According to the WHO recommendations this variant was named type Frankfurt (Gd Frankfurt).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01468536
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Über eine neue erythrocytäre Glucose-6-Phosphatdehydrogenase-Variante, ‚Typ Frankfurt‘ (1974)
    Springer
    Journal of molecular medicine 52 (1974), S. 485-492 
    Details
    ISSN: 1432-1440
    Keywords: New erythrocyte G-6-PD variant ; Gd Frankfurt ; Structural abnormality ; Molecular weight ; Peptide analysis ; Amino acid substitution ; Lys → Glu ; Neue erythrocytäre G-6-PD-Variante ; Gd Frankfurt ; strukturelle Anomalie ; Molekulargewicht ; Peptidanalyse ; Aminosäurenaustausch ; Lys → Glu
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Eine neue, anomale erythrocytäre G-6-PD-Variante, Gd Frankfurt, wurde nach chromatographischer Reingung auf DEAE-Cellulose, durch fraktionierte Ammoniumsulfat-Fällung und zweimalige Gelfiltration auf das rund 14000fache angereichert. Mittels Gelfiltration wurde eine Molekulargewichtsbestimmung durchgeführt, ferner wurde der SH-Gruppen-Gehalt und die Hemmung der Aktivität durch N-Äthylmaleimid bestimmt. Im Vergleich zum Normalenzym, Gd B, fand sich — bei gleichem SH-Gruppen-Gehalt — ein von der Norm nur geringfügig abweichendes Molekulargewicht von 223 000 gegenüber 243 500 beim Normalenzym und eine etwas stärkere Hemmung durch N-Äthylmaleimid. Nach tryptischer Verdauung ergab die Peptidanalyse mittels Fingerprint-Verfahrens auf Kieselgel-S-Dünnschichtplatten ein abweichendes Verhalten für 1 Peptid, während die restlichen 39 Peptide die gleiche Lokalisation aufwiesen. Die Aminosäuren-Analyse dieser differienden Peptide deckte für die neue Variante einen Austausch von Lysin gegen Glutaminsäure auf.
    Notes: Summary A new, abnormal erythrocyte G-6-PD variant, Gd Frankfurt, was first purified chromatographically on DEAE cellulose. Further purification was performed by fractionate precipitation with ammonium sulfate and by double gel filtration on Sephadex G-200. By these procedures a nearly 14000-fold concentration was obtained. In this preparation as well as in a control preparation of the normal enzyme variant Gd B the molecular weight, the content of sulfhydryl groups and the inhibition of enzyme activity by N-ethylmaleimide was determined. The content of sulfhydryl groups was found to be the same as in the normal enzyme variant. The molecular weights are slightly different: for the abnormal enzyme variant the value obtained was 223 000, and 243 500 for the normal enzyme. The inhibition by N-ethyl-maleimide showed to be somewhat stronger in the abnormal variant than in the normal enzyme. Peptide analysis after tryptic digestion was performed by fingerprint technique on silica gel-starch thin layers. 39 peptides of the abnormal variant showed the same pattern as in the normal enzyme whereas one peptide was found in a differing localization. Amino acid analysis' of the differing peptides revealed a substitution of glutamic acid for lysine in the abnormal enzyme variant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01468537
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Serum antibodies against gliadin and reticulin in a family study of coeliac disease (1980)
    Springer
    European journal of pediatrics 135 (1980), S. 31-36 
    Details
    ISSN: 1432-1076
    Keywords: Antigen handling ; Coeliac disease ; Family study ; Fluorescent antibody technique ; Gliadin antibodies ; Reticulin antibodies ; Monozygotic twins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The familial occurence of coeliac disease is well known. In every day practice, however, diagnosis of coeliac disease is not frequently established in the relatives of patients. As it did not seem practicable to biopsy all relatives, several tests were investigated in selecting individuals for intestinal biopsy in a family study. 55 index patients out of 54 families with biopsy-proven coeliac disease and 165 of their first grade relatives underwent the study. Immunofluorescent gliadin and reticulin antibodies were determined, and additionally laboratory tests were done. These included haemoglobin, serum iron, serum protein and albumin, serum immunoglobulins and blood xylose. The immunofluorescent gliadin antibody assay using red cells coated with gliadin proved to be superior to the other methods. False negatives came to 8.7%, and false positives 10.9%, in healthy relatives. Gliadin antibodies could be found five times more frequently in healthy relatives than in normal controls. This finding indicates a genetic predisposition to the formation of gliadin antibodies in coeliac families. Ninety-one percent of index coeliac children had IgG-antigliadin in their sera while on a normal diet. During gluten-free diet, and in adult patients, results were less convincing. All relatives with antigliadin titres greater than 8 have been biopsied, and all with titres above 64 were shown to have coeliac disease. The prevalence of coeliac disease found in this study was 5.5%. In the active state of coeliac disease in children, gliadin antibody determination thus is a valuable diagnostic tool but in selecting relatives for biopsy there are limitations to the wide application of the test. Although reticulin antibodies are more specific for coeliac disease than gliadin antibodies, determination of antireticulin proved to be much less sensitive.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00445889
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    Paper (German National Licenses)
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