Structural Effects in the Self-Association of γ II-Crystallin

  • P. Stiuso
  • D. Pulcini
  • A. La Pegna
  • C. Roscigno
  • R. Ragone
  • G. Colonna
Chapter
Part of the Experimental Biology and Medicine book series (EBAM, volume 19)

Abstract

The eye lens is a proteic glass, the properties of which depend on the supramolecular organization of lens specific proteins, the α-, β- and γ-crystallins (1). In order to understand this proteic system, it is necessary first to describe the intermolecular interactions among crystallins and then consider the behavior of this complex framework in normal and/or pathological states, e.g. cataracts (1). Such interactions are of importance in driving the steric arrangement of the proteins inside the lens.

Keywords

Tyrosine Tryptophan Cataract Tyrosyl 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Molecular and Cellular Biology of the Eye Lens (1981) (Bloemendal, H., ed.) J. Wiley, New York.Google Scholar
  2. 2.
    Siezen, R.J. and Owen, E.A. (1981) Biophys. Chem. 18, 181–194.CrossRefGoogle Scholar
  3. 3.
    Bjork, I. (1964) Exp. Eye Res. 3, 254.CrossRefGoogle Scholar
  4. 4.
    Wetlaufer, D. (1962) Advan. Protein Chem. 17, 303.CrossRefGoogle Scholar
  5. 5.
    Chen, R.F., Edelhoch, H. and Steiner, R.F. (1969) in: Physical Principles and Techniques of Protein Chemistry (Leach, S.J., ed.) pp. 171–244, Academic Press, New York.Google Scholar

Copyright information

© The Humana Press Inc. 1987

Authors and Affiliations

  • P. Stiuso
    • 1
  • D. Pulcini
    • 1
  • A. La Pegna
    • 1
  • C. Roscigno
    • 1
  • R. Ragone
    • 1
  • G. Colonna
    • 1
  1. 1.Istituto di Chimica e Chimica Biologica, I Facoltà di MedicinaUniversità di NapoliItaly

Personalised recommendations