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Über die isoelektrische Trennung von Serumalbuminen

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Zusammenfassung

Am Beispiel des Albumins wird die isoelektrische Trennung von Bluteiweißkörpern auf Trägerampholyten demonstriert. Mit der Methode ließ sich eine Auftrennung des Albumins in mehrere Komponenten mit unterschiedlichen isoelektrischen Punkten erreichen. Die verschiedenen Fraktionen verteilen sich hinsichtlich ihres isoelektrischen Punktes über den pH-Bereich pH 4,7–5,6. Die Ursachen dieser Heterogenität werden im Zusammenhang mit der entsprechenden Literatur diskutiert.

Weiterhin werden die Ergebnisse der isoelektrischen Trennung131J-markierten Albumins mitgeteilt. Es zeigt sich, daß die Markierung das isoelektrische Muster des Albumins qualitativ nicht verändert. Die Bedeutung der radioaktiven Markierung von Proteinen für die Auswertung der isoelektrischen Trennung wird besprochen.

Summary

Human serum albumin has been fractionated by isoelectric focussing. By this method several components of albumin could be separated according to their isoelectric points, which ranged between pH 4.7–5.6.

In addition the results of isoelectric focussing of131J-marked human albumin were communicated. It could be demonstrated that the radioactive marking don't alter qualitatively the isoelectric distribution of human serum albumin. The significance of the radioactive marking of proteins for isoelectric focussing is discussed.

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Authors and Affiliations

  1. Klinik und Lehrstuhl für Innere Medizin der Ruhr-Universität Bochum (Klinikum Essen), Germany

    H. E. Reis & O. Wetter

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  1. H. E. Reis
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  2. O. Wetter
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Reis, H.E., Wetter, O. Über die isoelektrische Trennung von Serumalbuminen. Klin Wochenschr 47, 426–430 (1969). https://doi.org/10.1007/BF01745788

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