Changes in proteins of the human lens in development and aging.
A number of proteins have been isolated from the human lens at different stages of development, from before birth to old age. These proteins have been characterized and compared with each other and with corresponding proteins from bovine lens. Many similarities were found between human and bovine crystallins, but alpha-crystallin isolated from old human lenses using DEAE-cellulose, unlike bovine alpha-crystallin similarly isolated, is not found as large soluble aggregates. The amide contents of various lens protein fractions were determined. No extensive changes were found during adult life, but there was evidence that significant deamidation of alpha-crystallin had occurred before birth and possibly during infancy. The results are related to the unique development and aging of the lens.
D000293:Adolescent; D000328:Adult; D000368:Aged; D000375:Aging; D000577:Amides / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002234:Carbodiimides; D002417:Cattle; D002675:Child, Preschool; D002848:Chromatography, DEAE-Cellulose; D003459:Crystallins / Q000032:analysis* / Q000302:isolation & purification; D004588:Electrophoresis, Cellulose Acetate; D005333:Fetus; D006801:Humans; D007908:Lens, Crystalline / Q000254:growth & development*; D008875:Middle Aged; D008970:Molecular Weight; D009646:Norleucine; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D000577:Amides; D000596:Amino Acids; D002234:Carbodiimides; D003459:Crystallins; D010446:Peptide Fragments; D009646:Norleucine; D014357:Trypsin