IOVS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schachar, R. A.
Right arrow Articles by Solin, S. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schachar, R. A.
Right arrow Articles by Solin, S. A.

Investigative Ophthalmology & Visual Science, Vol 14, 380-396, Copyright © 1975 by Association for Research in Vision and Ophthalmology

ARTICLES AND REPORTS

The microscopic protein structure of the lens with a theory for cataract formation as determined by Raman spectroscopy of intact bovine lenses

RA Schachar and SA Solin

Intact bovine lenses have been studied using the polarized Raman spectroscopic technique. A brief theoretical and experimental review of Raman spectroscopy is presented. From the dependence of the Raman depolarization ratio on the propagation direction of the incident radiation we have determined that the uniaxial qualities of the lens result from microscopic anisotropy and have established the quantitative positional correlation of specific chemical bonds with respect to the lens optic axis. In particular, the hydrogen bonded linear CONH groups of the antiparallel beta-pleated sheet are preferentially oriented in directions orthogonal to the lens optic axis. The Raman spectra of intact lenses do not exhibit bands at positions characteristic of either the alpha-helix or the random coil protein structure. The antiparallel beta-pleated sheet protein microstructure and the lens fiber cross-sectional macrostructure exhibit a remarkable similarity. This similarity may be causal and is consistent with the protein concentration of the lens, the birefringent properties observed by both Lenhard and Brewster, the CONH bond angle distribution with respect to the optic axis, and the lens anatomy. It is suggested that cortical cataracts are caused by fluctuations in protein orientational order.


This article has been cited by other articles:


Home page
 IOVSHome page
J. Han and K. L. Schey
MALDI Tissue Imaging of Ocular Lens {alpha}-Crystallin.
Invest. Ophthalmol. Vis. Sci., July 1, 2006; 47(7): 2990 - 2996.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1975 by the Association for Research in Vision and Ophthalmology