The photolysis of lens fiber membranes.
Calf lens fiber membranes were photolyzed in the presence and absence of sensitizers and scavengers. Photolytic damage was assessed by SDS-polyacrylamide gel electrophoresis, UV and fluorescence spectra and amino acid analyses. With irradiation, there is an apparent polymerization of the major membrane polypeptide (MP26) and the formation of material which does not enter SDS-polyacrylamide gels. Some degradation was also observed. These changes are accompanied by losses of histidine and tryptophan and changes in the UV spectra. The rate of photolysis is enhanced in the presence of the glucoside of 3-hydroxykynurenine (3-OH-KYN), a compound endogenous to the lens. The reaction is retarded in the presence of sulfhydryl-containing compounds such as glutathione.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D020346:Aquaporins; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D005136:Eye Proteins / Q000528:radiation effects; D005978:Glutathione / Q000494:pharmacology; D006639:Histidine / Q000032:analysis; D066298:In Vitro Techniques; D007737:Kynurenine / Q000031:analogs & derivatives / Q000494:pharmacology; D007904:Lens Cortex, Crystalline / Q000032:analysis / Q000528:radiation effects*; D007908:Lens, Crystalline / Q000528:radiation effects*; D008562:Membrane Glycoproteins; D010782:Photolysis; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013997:Time Factors; D014364:Tryptophan / Q000032:analysis
D000596:Amino Acids; D020346:Aquaporins; D005136:Eye Proteins; D008562:Membrane Glycoproteins; C030328:aquaporin 0; C005045:3-hydroxykynurenine; D007737:Kynurenine; D006639:Histidine; D014364:Tryptophan; D005978:Glutathione