Isolation and physical characterization of bovine lens crystallins.

@article{Chiou1979IsolationAP,
  title={Isolation and physical characterization of bovine lens crystallins.},
  author={S. H. Chiou and Parviz Azari and Michael E. Himmel and Phil G. Squire},
  journal={International journal of peptide and protein research},
  year={1979},
  volume={13 4},
  pages={
          409-17
        }
}
The soluble proteins from bovine lens homogenate were separated on Sepharose CL-6B (2 X 200 cm) in 0.05 M tris-NaHSO3 pH 8.2 buffer containing 20 mM EDTA. Five sharp and defined fractions (HM alpha, alpha, beta H, beta L, gamma) were obtained. Each crystallin fraction was further purified by rechromatography on the same column. Each protein fraction was pure as judged by ultracentrifugation and SDS-gel electrophoresis. The molecular weights of the five fractions were 3.04 x 10(6), 5.83 x 10(5… CONTINUE READING

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Cardiac alpha-crystallin

  • Molecular and Cellular Biochemistry
  • 1990
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