Proline‐ and alanine‐rich N‐terminal extension of the basic bovine β‐crystallin B1 chains
- 19 September 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 161 (2) , 225-229
- https://doi.org/10.1016/0014-5793(83)81013-8
Abstract
The amino acid sequence of the N-terminal region of the two basic bovine β-crystallin B1 chains has been analyzed. The results reveal that βB1b is derived in vivo from the primary gene product βB1a by removal of a short N-terminal sequence. It appears that the βB1 chains have the same domain structure as observed in other β- and γ-crystallin chains. They have, however, a very long N-terminal extension in comparison with other β-chains. This extension is mainly composed of a remarkable Pro- and Ala-rich sequence, which suggests an interaction of these structural proteins with the cytoskeleton and/or the plasma membranes of the lens cells.Keywords
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