Absicht der Studie war die elektrophoretische Untersuchung von Proteinen in Humanplasma, vor und nach der photodynamischen Virusinaktivierung mit dem Phenothiazinfarbstoff Methylenblau (MB). Die Ergebnisse der zweidimensionalen (2D-)Immunelektrophorese von unbehandeltem und photodynamisch behandel-tem Plasma zeigen, daβ die photodynamische Behandlung unter Routinebedingun-gen (1 µM MB und 1 h Belichtung) die elektrophoretische Beweglichkeit der geprüf-ten Plasmaproteine nicht beeinfluβt. Unter härteren Bedingungen (25 µM MB und 2 h Belichtung) kommt es dagegen teilweise zu Alterationen im Albumin und Transferrin, wie die 2D-Immunelektrophorese zeigt. Mit Hilfe der 2D-Immunoblottechnik konnten im photodynamisch behandelten und unbehandelten Humanplasma keine Unterschiede in Albumin, Transferrin, Fibrinogen und Histidin-reichem Glykoprotein nachgewiesen werden. Die Aminosäureanalyse demonstriert, daβ es keine signifikanten Alterationen in den Aminosäuren der Plasmaproteine von unbehandeltem und unter Routinebedingungen behandeltem Plasma gibt. Lysin ist die einzige Aminosäure von Plasmaproteinen, die unter den oben genannten extremen Bedingungen alteriert wird.

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