The endopeptidase-resistant protein fraction from human cataractous lenses.
With aging and cataract formation, modifications in absorption and fluorescence of the human lens proteins are observed. These changes have been investigated by the examination of the endopeptidase-resistant fraction isolated from human cataractous lenses. This fraction is highly enriched in atypical fluorescence and absorption (i.e. not attributable to tryptophan, tyrosine or phenylalanine). It has a molecular weight of approximately 3000, is enriched in acidic amino acids and has only a 280 nm shoulder in its u.v. spectrum. The material does not contain detectable levels of malondialdehyde or N-formylkynurenine. Upon acid hydrolysis the fluorescence and u.v. spectra remain unchanged with only a minor degree of cleavage observed. Structural studies on some of the cleavage products indicated the presence of oxindolyl alanine and kynurenine. These compounds could result from photo-oxidation of tryptophan.
D000596:Amino Acids / Q000032:analysis; D002386:Cataract / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003459:Crystallins / Q000378:metabolism*; D010450:Endopeptidases; D006801:Humans; D066298:In Vitro Techniques; D007737:Kynurenine / Q000032:analysis; D000078183:Oxindoles; D013053:Spectrophotometry; D014364:Tryptophan / Q000031:analogs & derivatives / Q000032:analysis
D000596:Amino Acids; D003459:Crystallins; D000078183:Oxindoles; C011963:beta-3-oxindolylalanine; D007737:Kynurenine; D014364:Tryptophan; D010450:Endopeptidases