|
|
||||||||
Investigative Ophthalmology & Visual Science, Vol 28, 1157-1163, Copyright © 1987 by Association for Research in Vision and Ophthalmology
ARTICLES AND REPORTS |
GJ Bessems, E Keizer, J Wollensak and HJ Hoenders
The soluble proteins of a newborn human lens exhibit almost no non- tryptophan fluorescence. On aging, an increase in the fluorescence of all native crystallins is found except for gamma 2-crystallin. With formation of nuclear cataract, a further increase is seen for gamma 1- crystallin. The fluorophore, excitation 355 nm/emission 420 nm, is mainly associated with one species of the gamma 1-crystallin population. It is also present as such in the soluble fraction and increases significantly with nuclear cataract formation. At least one of the gamma 1-crystallins seems to play an important role in the cataractogenic process.
This article has been cited by other articles:
![]() |
S. Vazquez, J. A. Aquilina, J. F. Jamie, M. M. Sheil, and R. J. W. Truscott Novel Protein Modification by Kynurenine in Human Lenses J. Biol. Chem., February 8, 2002; 277(7): 4867 - 4873. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. D. Hood, B. Garner, and R. J. W. Truscott Human Lens Coloration and Aging. EVIDENCE FOR CRYSTALLIN MODIFICATION BY THE MAJOR ULTRAVIOLET FILTER, 3-HYDROXY-KYNURENINE O-beta -D-GLUCOSIDE J. Biol. Chem., November 12, 1999; 274(46): 32547 - 32550. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |