Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates.

@article{Sasaki1984ComparativeSA,
  title={Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates.},
  author={Tomoko Sasaki and Takeshi Kikuchi and Noboru Yumoto and Natsue Yoshimura and Takashi Murachi},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 20},
  pages={12489-94}
}
Homogeneous porcine calpain (Ca2+-dependent cysteine proteinase) was found to hydrolyze a variety of peptides and synthetic substrates. Leu-Trp-Met-Arg-Phe-Ala, eledoisin-related peptide, alpha-neoendorphin, angiotensin I, luteinizing hormone-releasing hormone, neurotensin, dynorphin, glucagon, and oxidized insulin B chain were cleaved with a general preference for a Tyr, Met, or Arg residue in the P1 position preceded by a Leu or Val residue in the P2 position. No great difference in… CONTINUE READING

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References

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Calcium and Cell Function (Cheung

T. Murachi
W. Y., ed) • 1983

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