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Investigation of single protein adsorption on ion exchangers using confocal laser scanning microscopy

✍ Scribed by M Ahmed; D L Pyle

Publisher
Wiley (John Wiley & Sons)
Year
1999
Tongue
English
Weight
174 KB
Volume
74
Category
Article
ISSN
0268-2575

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✦ Synopsis

Currently there are many ion exchangers available for protein puriücation, but there is little information on how efficiently the ion exchanger surface is used for protein binding. In this work we present the results from a confocal scanning laser microscope study of two anion exchangers, DEAE Toyopearl and Express Ion-Q, after equilibration with protein dye conjugates BSA-BODIPY FL and ovalbumin-Texas Red. The pictures and intensity proüles of DEAE Toyopearl show that both proteins bind preferentially to the surface compared with the core of the spherical ion exchangers. Results on the cylindrical shaped Express Ion-Q with BSA show a similar result but with ovalbumin-Texas Red constant protein binding is observed throughout the adsorbent. Confocal microscopy is demonstrated to be an excellent tool to discriminate between diþ erent ion exchangers for the optimisation of protein puriücation.

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