The complete amino acid sequences of two serine proteinase inhibitors from the fruiting bodies of a basidiomycete, Pleurotus ostreatus.

@article{Dohmae1995TheCA,
  title={The complete amino acid sequences of two serine proteinase inhibitors from the fruiting bodies of a basidiomycete, Pleurotus ostreatus.},
  author={Naoshi Dohmae and Koji Takio and Yoichi Tsumuraya and Yoshiteru Hashimoto},
  journal={Archives of biochemistry and biophysics},
  year={1995},
  volume={316 1},
  pages={498-506}
}
The complete amino acid sequences of two isomeric endogenous inhibitors, IA-1 and IA-2, both of which specifically inhibit an intracellular serine proteinase (proteinase A) purified from the fruiting bodies of a higher basidiomycete, Pleurotus ostreatus, were determined. Both inhibitors are acidic polypeptides with respective molecular masses of 8307 and 8244 Da, as determined by plasma desorption mass spectral analyses, and their N-terminal serine residue is blocked by acetylation. The… CONTINUE READING
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