Studies on lens proteins of mice with hereditary cataract. I. Comparative studies on the chemical and immunochemical properties of the soluble proteins of cataractous and normal mouse lenses.
Total soluble and insoluble proteins of the lens were similar in normal and hereditary cataractous mice up to 1 week of age. Thereafter, the normal mouse lens showed a continued increase in weight and protein content until 500 days of age. In cataractous mice, while the total protein content increased up to 60 days and reached a plateau, the soluble protein content declined dramatically from day 22 to day 60, and then the rate of decrease remained constant up to 500 days. At different ages, the soluble proteins were separated by gel filtration into the high molecular weight proteins, alpha-, beta- and gamma-crystallin fractions. All of these showed an age-related increase in the normal lens, and the relative values of alpha- and beta-crystallins increased for a 410-day period. On the other hand, in the cataractous process, the high molecular weight protein increased, and alpha-, beta- and gamma-crystallins decreased: the degree was especially marked in gamma-crystallin. Immunochemical studies indicated that the aggregation of beta-crystallin occurred much earlier in the cataractous lens than in the normal. Analysis of the amino acid composition and ultraviolet absorption spectra revealed no significant chemical differences between the crystallins of the normal and the cataractous lens.
D000375:Aging; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000831:Animals, Newborn; D002386:Cataract / Q000235:genetics / Q000378:metabolism*; D003459:Crystallins / Q000302:isolation & purification / Q000378:metabolism*; D007122:Immunoelectrophoresis; D007908:Lens, Crystalline / Q000473:pathology; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight; D012995:Solubility
D000596:Amino Acids; D003459:Crystallins