PubMed1982
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.