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Physical-chemical characterization of the different individual cortical alfa-crystallin fractions from bovine lenses

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Analytical Ultracentrifugation

Part of the book series: Progress in Colloid & Polymer Science ((PROGCOLLOID,volume 99))

Abstract

The soluble bovine eye lens cytoplasm has been separated in its α-, β- and γ-crystallin fractions, using size exclusion chromatography. The individual α-crystallin fractions have been characterized using moving boundary and equilibrium sedimentation and photon correlation spectroscopy. The α-crystallin fractions represent a very broad distribution in molar mass from 500 000 to 1 100 000 g/mole, with a maximum at 650 000 g/mole. This population contains also a broad distribution of hydrodynamic structures, ranging from compact to more asymmetric structures; the main population has a frictional coefficient f/f 0 ratio of (1.45±0.05). These structural properties perfectly fit the micellar model.

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Authors and Affiliations

  1. Biophysics Research Group Department of Biochemistry, University of Antwerp, Universiteitsplein 1, 2610, Antwerp, Belgium

    T. Aerts, Q. H. Wang, S. Tatarkova & J. Clauwaert

Authors
  1. T. Aerts
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  2. Q. H. Wang
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  3. S. Tatarkova
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  4. J. Clauwaert
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J. Behlke

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© 1995 Dr. Dietrich Steinkopff Verlag GmbH & Co. KG

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Aerts, T., Wang, Q.H., Tatarkova, S., Clauwaert, J. (1995). Physical-chemical characterization of the different individual cortical alfa-crystallin fractions from bovine lenses. In: Behlke, J. (eds) Analytical Ultracentrifugation. Progress in Colloid & Polymer Science, vol 99. Steinkopff. https://doi.org/10.1007/BFb0114076

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  • DOI: https://doi.org/10.1007/BFb0114076

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  • Publisher Name: Steinkopff

  • Print ISBN: 978-3-7985-1038-8

  • Online ISBN: 978-3-7985-1666-3

  • eBook Packages: Springer Book Archive

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