Proline- and alanine-rich N-terminal extension of the basic bovine beta-crystallin B1 chains.

@article{Berbers1983ProlineAA,
  title={Proline- and alanine-rich N-terminal extension of the basic bovine beta-crystallin B1 chains.},
  author={Guy A. M. Berbers and W. A. de Haard Hoekman and Hans Bloemendal and Wilfried W. de Jong and Traute Kleinschmidt and Gerhard Braunitzer},
  journal={FEBS letters},
  year={1983},
  volume={161 2},
  pages={225-9}
}
The amino acid sequence of the N-terminal region of the two basic bovine beta-crystallin B1 chains has been analyzed. The results reveal that beta B1b is derived in vivo from the primary gene product beta B1a by removal of a short N-terminal sequence. It appears that the beta B1 chains have the same domain structure as observed in other beta- and gamma-crystallin chains. They have, however, a very long N-terminal extension in comparison with other beta-chains. This extension is mainly composed… CONTINUE READING

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