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Sequence homologies between tonin, nerve growth factor γ-subunit, epidermal growth factor-binding protein and serine proteases

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Abstract

Tonin1, a protein isolated from rat submaxillary gland, has interesting proteolytic activities. It is able to liberate angiotensin II from angiotensinogen (or a shorter synthetic tetradecapeptide corresponding to the first 14 residues) and from angiotensin I; it is also able to release peptides from β-lipotropin (β-LPH), corticotropin (ACTH) and their common precursor proopiomelanocortin (POMC) leaving intact the β-endorphin and the Met-enkephalin entities2,3. Here, we describe the sequencing of 95 of the 272 amino acids of tonin. Our results reveal extensive sequence homology of tonin with the γ-subunit of nerve growth factor (NGF) and epidermal growth factor (EGF)-binding protein (both of which also have proteolytic activities), and also with serine proteases.

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References

  1. Demassieux, S., Boucher, R., Grisé, C. & Genest, J. Can. J. Biochem. 54, 788–795 (1976).

    Article  CAS  Google Scholar 

  2. Seidah, N. G. et al. Biochem. biophys. Res. Commun. 86, 1002–1013 (1979).

    Article  CAS  Google Scholar 

  3. Seidah, N. G. et al. in Proc. 6th Am. Peptide Symp. (eds Gross, E. & Meienhofer, J.) 921–924 (Pierce Chemical Company, 1979).

  4. Seidah, N. G. et al. Can. J. Biochem. 56, 920–925 (1978).

    Article  CAS  Google Scholar 

  5. Thomas, K. A., Baglan, N. C. & Bradshaw, R. A. J. biol. Chem. (in the press).

  6. Kurosky, A. et al. Proc. natn. Acad. Sci. U.S.A. 77, 3388–3392 (1980).

    Article  ADS  CAS  Google Scholar 

  7. Dayhoff, M. D. (ed.) Atlas of Protein Sequence and Structure Vol.5, suppl. 3 (1978).

  8. Mole, J. E. & Niemann, M. A. J. biol. Chem. 255, 8472–8476 (1980).

    CAS  PubMed  Google Scholar 

  9. Christie, D. L., Gagnon, J. & Porter, R. R. Proc. natn. Acad. Sci. U.S.A. 77, 4923–4927 (1980).

    Article  ADS  CAS  Google Scholar 

  10. Walz, D. A., Hewett-Emmett, D. & Siegers, W. H. Proc. natn. Acad. Sci. U.S.A. 74, 1969–1972 (1977).

    Article  ADS  CAS  Google Scholar 

  11. Butkowski, R. J., Elion, J., Downing, M. R. & Mann, K. G. J. biol. Chem. 252, 4942–4957 (1977).

    CAS  PubMed  Google Scholar 

  12. Woodbury, R. G., Katunuma, N., Kobayashi, K., Titani, K. & Neurath, H. Biochemistry 17, 811–819 (1978).

    Article  CAS  Google Scholar 

  13. Volanakis, J. E., Bhown, A. S., Bennett, J. C. & Mole, J. E. Proc. natn. Acad. Sci. U.S.A. 77, 1116–1119 (1980).

    Article  ADS  CAS  Google Scholar 

  14. Bradshaw, R. A. A. Rev. Biochem. 47, 191–216 (1978).

    Article  CAS  Google Scholar 

  15. Thoenen, H. & Barde, Y.-A. Physiol. Rev. 60, 1284–1335 (1980).

    Article  CAS  Google Scholar 

  16. Eur. J. Biochem. 5, 151–153 (1968).

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Lazure, C., Seidah, N., Thibault, G. et al. Sequence homologies between tonin, nerve growth factor γ-subunit, epidermal growth factor-binding protein and serine proteases. Nature 292, 383–384 (1981). https://doi.org/10.1038/292383a0

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