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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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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