Abstract
Salmon calcitonin (sCT) is an example of one of the many bioactive peptides that require amidation of the carboxy terminus for full potency. We describe a method for the production of amidated sCT in the mammary gland of transgenic rabbits. Expression of a fusion protein comprising human alpha lactalbumin joined by an enterokinase cleavable linker to sCT was directed to the mammary gland under the control of the ovine beta lactoglobulin promoter. C-terminal amidation in vivo was achieved by extending the sCT by a single glycine residue that provides a substrate for endogenous amidating activity in the mammary gland. Full characterization of the released sCT demonstrated it to be equivalent to synthetic standard in terms of structure, purity, and potency.
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McKee, C., Gibson, A., Dalrymple, M. et al. Production of biologically active salmon calcitonin in the milk of transgenic rabbits. Nat Biotechnol 16, 647–651 (1998). https://doi.org/10.1038/nbt0798-647
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DOI: https://doi.org/10.1038/nbt0798-647
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