Studies on the water-soluble lens proteins of the lizard,Calotes versicolor. II. Electrophoretic and immunological characterization
✍ Scribed by Pal, J. K. ;Nerurkar, A. R. ;Goel, S. C.
- Publisher
- John Wiley and Sons
- Year
- 1982
- Tongue
- English
- Weight
- 595 KB
- Volume
- 224
- Category
- Article
- ISSN
- 0022-104X
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✦ Synopsis
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.