Phosphorescence measurements of calf γ-II, III, and IV crystallins at 77 and 293 K
Author:
Publisher
Elsevier BV
Subject
Cellular and Molecular Neuroscience,Sensory Systems,Ophthalmology
Reference48 articles.
1. Conformational changes of bovine lens crystallins in a photodynamic system;Andley;Photochem. Photobiol.,1986
2. Quenching of tryptophan fluorescence in bovine lens proteins by acrylamide and iodide;Augusteyn;Curr. Eye Res.,1988
3. Studies on γ-crystallin from calf lens. I. Isolation by gel filtration;Björk;Exp. Eye Res.,1961
4. Studies on γ-crystallin from calf lens. II. Purification and some properties of the main protein components;Björk;Exp. Eye Res.,1964
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1. Probing the microenvironments of tryptophan residues in the monomeric crystallins of the bovine lens;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1994-03
2. Picosecond fluorescence decay of lens protein γ-II crystallin;Biophysical Chemistry;1993-10
3. THE ANAEROBIC PHOTOLYSIS OF LENS α-CRYSTALLIN: EVIDENCE FOR TRIPLET STATE MEDIATED PHOTODAMAGE;Photochemistry and Photobiology;1990-10
4. THE RATES OF PHOTOLYSIS OF THE FOUR INDIVIDUAL TRYPTOPHAN RESIDUES IN UV EXPOSED CALF γ-II CRYSTALLIN;Photochemistry and Photobiology;1990-03
5. Excited triplet states used to study biological macromolecules at room temperature;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1989-08
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