Cleavage specificity of a proteolytic antibody light chain and effects of the heavy chain variable domain.

@article{Sun1997CleavageSO,
  title={Cleavage specificity of a proteolytic antibody light chain and effects of the heavy chain variable domain.},
  author={May Sun and Q. S. Gao and L Kirnarskiy and Anthony R. Rees and Sudhir Paul},
  journal={Journal of molecular biology},
  year={1997},
  volume={271 3},
  pages={374-85}
}
The recombinant light chain (L chain) of an antibody raised by immunization with vasoactive intestinal polypeptide (VIP) cleaved this peptide on the C-terminal side of basic residues. The major sites of cleavage in VIP were two adjacent peptide bonds, Lys20-Lys21 and Lys21-Tyr22. Lower levels of cleavage were evident at Arg14-Lys15 and Lys15-Gln16. Hydrolysis of radiolabeled VIP by the L chain was inhibited by two serine protease inhibitors, diisopropylfluorophosphate and aprotinin, but not by… CONTINUE READING

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