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- W2036682711 abstract "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 α-crystallin which cross-reacts with chick α, 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 β -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 δ-crystallin in addition to βH crystallin or that Calotes βH has a high molecular weight subunit like human βH; however, in immunological tests no material cross-reacting with chick δ was seen. C4 and C5 are low molecular weight, monomeric, and basic proteins which in all probability are not γ-crystallins." @default.
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- W2036682711 date "1982-12-30" @default.
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- W2036682711 title "Studies on the water-soluble lens proteins of the lizard,Calotes versicolor. II. Electrophoretic and immunological characterization" @default.
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- W2036682711 doi "https://doi.org/10.1002/jez.1402240303" @default.
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