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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Demassieux, S., Boucher, R., Grisé, C. & Genest, J. Can. J. Biochem. 54, 788–795 (1976).
Seidah, N. G. et al. Biochem. biophys. Res. Commun. 86, 1002–1013 (1979).
Seidah, N. G. et al. in Proc. 6th Am. Peptide Symp. (eds Gross, E. & Meienhofer, J.) 921–924 (Pierce Chemical Company, 1979).
Seidah, N. G. et al. Can. J. Biochem. 56, 920–925 (1978).
Thomas, K. A., Baglan, N. C. & Bradshaw, R. A. J. biol. Chem. (in the press).
Kurosky, A. et al. Proc. natn. Acad. Sci. U.S.A. 77, 3388–3392 (1980).
Dayhoff, M. D. (ed.) Atlas of Protein Sequence and Structure Vol.5, suppl. 3 (1978).
Mole, J. E. & Niemann, M. A. J. biol. Chem. 255, 8472–8476 (1980).
Christie, D. L., Gagnon, J. & Porter, R. R. Proc. natn. Acad. Sci. U.S.A. 77, 4923–4927 (1980).
Walz, D. A., Hewett-Emmett, D. & Siegers, W. H. Proc. natn. Acad. Sci. U.S.A. 74, 1969–1972 (1977).
Butkowski, R. J., Elion, J., Downing, M. R. & Mann, K. G. J. biol. Chem. 252, 4942–4957 (1977).
Woodbury, R. G., Katunuma, N., Kobayashi, K., Titani, K. & Neurath, H. Biochemistry 17, 811–819 (1978).
Volanakis, J. E., Bhown, A. S., Bennett, J. C. & Mole, J. E. Proc. natn. Acad. Sci. U.S.A. 77, 1116–1119 (1980).
Bradshaw, R. A. A. Rev. Biochem. 47, 191–216 (1978).
Thoenen, H. & Barde, Y.-A. Physiol. Rev. 60, 1284–1335 (1980).
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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DOI: https://doi.org/10.1038/292383a0
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