Conformational changes in human lens proteins in cataract.
The reactivity of protein thiol groups in human lens and the susceptibility of the proteins to tryptic digestion were investigated. Both were found to be greater in some cataractous lenses, indicating that lens proteins have unfolded during cataractogenesis. Almost all the tyrosine in the proteins of the normal human lens reacts with tetranitromethane and is therefore probably on the outside of the major lens proteins.
D000596:Amino Acids / Q000032:analysis; D002247:Carbon Isotopes; D002386:Cataract / Q000378:metabolism*; D002850:Chromatography, Gel; D003459:Crystallins / Q000378:metabolism*; D006801:Humans; D007525:Isoelectric Focusing; D008697:Methane; D009574:Nitro Compounds; D011487:Protein Conformation; D013438:Sulfhydryl Compounds; D014357:Trypsin; D014443:Tyrosine
D000596:Amino Acids; D002247:Carbon Isotopes; D003459:Crystallins; D009574:Nitro Compounds; D013438:Sulfhydryl Compounds; D014443:Tyrosine; D014357:Trypsin; D008697:Methane