Studies on the water-soluble lens proteins of the lizard, Calotes versicolor. II. Electrophoretic and immunological characterization.
The Sephadex G-200 gel filtration fractions C1 to C6 of the water-soluble lens proteins of Calotes versicolor have been characterized by polyacrylamide gel electrophoresis (PAGE), 7 M urea PAGE, SDS PAGE, and immunological tests. C1 fraction, an alpha-crystallin which cross-reacts with chick alpha, has very low amount of B chains. It shows two bands in SDS PAGE, one strong and another weak. C2 and C3 fractions, both of which partially cross-react with chick beta-crystallins, are largely similar but not identical. C2 in SDS PAGE produces a faint band with a molecular weight of 54,500, which suggests that C2 may either contain a small amount of delta-crystallin in addition to beta H crystallin or that Calotes beta H has a high molecular weight subunit like human beta H; however, in immunological tests no material cross-reacting with chick delta was seen. C4 and C5 are low molecular weight, monomeric, and basic proteins which in all probability are not gamma-crystallins.
D000818:Animals; D002645:Chickens; D003459:Crystallins / Q000276:immunology / Q000302:isolation & purification*; D004588:Electrophoresis, Cellulose Acetate; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000276:immunology; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D008116:Lizards / Q000378:metabolism*; D013045:Species Specificity
D003459:Crystallins; D000939:Epitopes