Affinity gel electrophoresis as a predictive technique in the fractionation of transgenic sheep milk proteins by affinity aqueous two-phase partitioning |
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| Authors: | A.T. Andrews D.P. Harris G. Wright D.L. Pyle J.A. Asenjo |
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| Affiliation: | (1) Food Chemistry Group, School of Applied Sciences, University of Wales Institute, Cardiff (UWIC);(2) Food Science Department, New Zealand Dairy Research Institute, Private Bag 11029, Palmerston North;(3) PPL Therapeutics Ltd. Roslin, Midlothian, EH25 9PP Scotland, UK;(4) Department of Food Science & Technology, University of Reading, P.O. Box 226, Whiteknights, Reading;(5) Department of Chemical Engineering, Centre for Biochemical Engineering and Biotechnology, Chile |
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| Abstract: | Affinity electrophoresis in the presence of various triazine dyes of sheep milk proteins, including transgenically-introduced human  1-antitrypsin, has been evaluated as a predictive technique for possible large scale affinity-driven aqueous two-phase purifications. The success of the approach suggested it has potential as a general method for the rapid screening of ligands using only  g amounts of sample, that could be applied to many complex mixtures before embarking on more costly and time-consuming two-phase partitioning experiments. |
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| Keywords: | affinity electrophoresis milk protein transgenic aqueous two-phase systems triazine dyes |
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