-Crystallin. The isolation and characterization of distinct macromolecular fractions.
alpha-Crystallin was isolated from calf lens periphery by chromatography on DEAE-cellulose and gel filtration. Three distinct populations of macromolecules have been isolated with molecular weights in the ranges approx. 6x10(5)-9x10(5), 0.9x10(6)-4x10(6) and greater than 10x10(6). The concentration of macromolecules at the molecular-weight limits of a population are very low. The members of the different populations do not appear to be in equilibrium with each other. Further, in those molecular-weight fractions investigated, no equilibrium between members of the same population was observed. The population of lowest molecular weight comprises 65-75% of the total material. The amino acid and subunit composition of the different-sized fractions appear very similar, if not identical. The only chemical difference observed between the fractions is the presence of significant amounts of sugar in the higher-molecular-weight fractions. Subunit molecular weights of approx. 19.5x10(3) and 22.5x10(3) were observed for all alpha-crystallin fractions.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003459:Crystallins / Q000032:analysis / Q000302:isolation & purification*; D004586:Electrophoresis; D046911:Macromolecular Substances; D008970:Molecular Weight
D000596:Amino Acids; D003459:Crystallins; D046911:Macromolecular Substances