Photolytic changes in lens proteins
- 1 January 1984
- journal article
- research article
- Published by Taylor & Francis in Current Eye Research
- Vol. 3 (1), 145-158
- https://doi.org/10.3109/02713688408997196
Abstract
Many of the age related and cataractous changes that occur in the human lens may be due to some photolytic process. These include either the direct photolysis of lens protein or photosensitized reactions involving 3-OH Kyn glucoside. The extent to which these photochemical reactions play a role is determined by the level of lens oxygen and the presence of quenchers endogenous to the lens.Keywords
This publication has 23 references indexed in Scilit:
- PHOTOSENSITIZED OXIDATION IN THE OCULAR LENS: EVIDENCE FOR PHOTOSENSITIZERS ENDOGENOUS TO THE HUMAN LENSPhotochemistry and Photobiology, 1981
- THE ANAEROBIC PHOTOLYSIS OF TRYPTOPHAN CONTAINING PEPTIDES—IIPhotochemistry and Photobiology, 1981
- Nonenzymatic Browning in Vivo: Possible Process for Aging of Long-Lived ProteinsScience, 1981
- ULTRAVIOLET RADIATION IN THE AGING AND CATARACTOUS LENS: A Survey*Acta Ophthalmologica, 1978
- Fluorescence of Proteins in 6‐M Guanidine HydrochlorideEuropean Journal of Biochemistry, 1976
- Identification of β carbolines isolated from fluorescent human lens proteinsNature, 1976
- PHOTOSENSITIZING PROPERTIES OF N‐FORMYLKYNURENINE †Photochemistry and Photobiology, 1975
- Distribution of Fluorescence in the Human Cataractous LensOphthalmic Research, 1975
- The binding of photo-oxidized tryptophan to a lens gamma-crystallinExperimental Eye Research, 1973
- Photo-oxidation of lens proteins by sunlight in the presence of fluorescent derivatives of kynurenine, isolated from the human lensExperimental Eye Research, 1973