Abstract
Rabbit erythrocytes contain a soluble aspartyl β-carboxyl methyltransferase capable of specifically carboxyl methylating the β-carboxyl group of an internal aspartyl residue in the synthetic polypeptide eledoisin, a hypotensively active peptide from the cephalopodsEledone moschata andE. aldrovandi, and tetragastrin, the biologically active C-terminal tetrapeptide of human gastrin. However, the aspartyl residue in delta sleep-inducing peptide (DSIP) could not be carboxyl methylated, nor could glutamyl residues in any polypeptide tested.
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Gosselin, M.L., Liss, M. The carboxyl methylation of aspartyl residues in eledoisin and tetragastrin by rabbit erythrocyte aspartyl β-carboxyl methyltransferase. J Protein Chem 4, 129–132 (1985). https://doi.org/10.1007/BF01025372
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DOI: https://doi.org/10.1007/BF01025372