Interactions of lens proteins

作者: R.J. Siezen , E.A. Owen

DOI: 10.1016/0301-4622(83)80030-1

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摘要: Concentrated solutions of calf alpha-crystallin (up to 45 g/l) and gamma-crystallin 67 were subjected frontal exclusion chromatography at pH 7.3, ionic strength 0.17 20 degrees C. The experimental concentration dependence the weight-average partition coefficient was compared with theoretical expressions, which include considerations thermodynamic non-ideality effects, for a single solute undergoing reversible self-association. Two types association pattern examined, discrete dimerization indefinite results are consistent an self-association gamma-crystallin, governed by isodesmic constant 6.7 X 10(-3) l/g. alpha-Crystallin appears self-associate either very weakly, maximal 0.9 l/g, or not all; distinction depends on assessment coefficients. consequences excluded volume effects these equilibria high total protein discussed. Mixtures analyzed 14 sedimentation velocity 115 g/l): no interaction observed.

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