Division of Pharmacology and Therapeutics, Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 1N4, Canada
(Received 13 June 1977)
Several lines of circumstantial evidence suggest that the neurohypophysial hormones may be biosynthesized in the form of larger peptides (prohormones) which are degraded to the free hormones during passage of the neurosecretory granules from the hypothalamus to the neurohypophysis (Vogt, 1953; Sachs & Takabatake, 1964; Pickering, Jones & Burford, 1971). Furthermore, it has been suggested that the hormone carrier proteins, the neurophysins, may at some stage in the biosynthesis, form part of the putative prohormones (Hope & Pickup, 1974).
In cattle, arginine-vasopressin (AVP) is associated with bovine neurophysin II (Dean, Hope & Kazič, 1968), the complete amino acid sequence of which has been elucidated by Schlesinger, Capra & Walter (1974) and Wuu & Crumm (1976). In the present study, two dodecapeptide analogues of AVP in which the peptide chain was elongated
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