EC Number   |
Subunits |
Reference |
|---|
    4.3.2.1 | ? |
4 * 50000, SDS-PAGE |
34422 |
| 4.3.2.1 | ? |
x * 51663, calculation from nucleotide sequence |
34423 |
| 4.3.2.1 | ? |
x * 51944, calculation from nucleotide sequence |
34423 |
| 4.3.2.1 | ? |
x * 55000, SDS-PAGE |
34445 |
| 4.3.2.1 | hexamer |
5 or 6 * 39000, SDS-PAGE |
34431 |
| 4.3.2.1 | homotetramer |
- |
664119 |
| 4.3.2.1 | homotetramer |
4 * 50900, recombinant His-tagged enzyme, SDS-PAGE |
-, 728906 |
| 4.3.2.1 | More |
small heat shock protein, alphaA-crystallin, functions as a molecular chaperone, and enhances thermal stability of both delta-crystallin and ASL. Thermal unfolding of delta-crystallin or ASL in the presence of alphaA-crystallin follows a similar three-state model. A stable intermediate which retains about 30% alpha-helical structure is observed. Protection from thermal denaturation by alphaA-crystallin is by interaction with partly unfolded ASL to form high molecular weight heteroligomers. Aggregate formation of ASL is significantly reduced in the presence of alphaA-crystallin. The extent of protection of ASL at different ratios of alpahA-crystallin is described by hyperbolic curves, suggesting the preferential recognition of partly unfolded ASL by alphaA-crystallin |
714375 |
| 4.3.2.1 | pentamer |
5 or 6 * 39000, SDS-PAGE |
34431 |
| 4.3.2.1 | tetramer |
- |
663485 |
