Glutamyl endopeptidase of Bacillus intermedius, strain 3-19.

@article{Leshchinskaya1997GlutamylEO,
  title={Glutamyl endopeptidase of Bacillus intermedius, strain 3-19.},
  author={Inna Borisovna Leshchinskaya and E. V. Shakirov and E L Itskovitch and Nelly Pavlovna Balaban and Ayslu Mardanova and Margarita Rashidovna Sharipova and Mikhail Borisovich Viryasov and Galina Nikolaevna Rudenskaya and V. M. Stepanov},
  journal={FEBS letters},
  year={1997},
  volume={404 2-3},
  pages={241-4}
}
A homogeneous glutamyl endopeptidase splitting peptide bonds of glutamic, rarely of aspartic acid residues in peptides and proteins, was isolated from Bacillus intermedius 3-19 culture filtrate using chromatography on CM cellulose and Mono S. The enzyme molecular mass is equal to 29 kDa, pI 8.4. The protease is inhibited by diisopropylfluorophosphate. The enzyme, like other glutamyl endopeptidases, reveals two pH optima at pH 7.5 and 9.0 for casein and one at pH 8.0 for Z-Glu-pNA hydrolysis. A… CONTINUE READING

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