All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli.

@article{Emori1988AllFR,
  title={All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli.},
  author={Y. Emori and Hiroko Kawasaki and Shinobu Imajoh and Y. Minami and Koji Suzuki},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 5},
  pages={2364-70}
}
We have already determined the primary structure of the endogenous inhibitor for calcium-dependent protease (CANP inhibitor, calpastatin) from the cDNA sequence and revealed that the CANP inhibitor contains four internally repeating units which could be responsible for its multiple reactive sites (Emori, Y., Kawasaki, H., Imajoh, S., Imahori, K., and Suzuki… CONTINUE READING