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Oxytocin: Peptides
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Oxytocin is a peptide of nine amino acids (a nonapeptide). The sequence is cysteine - tyrosine - isoleucine - glutamine - asparagine - cysteine - proline - leucine - glycine (CYIQNCPLG). The cysteine residues form a sulfur bridge. Oxytocin has a molecular mass of 1007 daltons. One international unit (IU) of oxytocin is the equivalent of about 2 micrograms of pure peptide.
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Oxytocin is a peptide of nine amino acids (a nonapeptide). The sequence is cysteine - tyrosine - isoleucine - glutamine - asparagine - cysteine - proline - leucine - glycine. The cysteine residues form a sulfur bridge. The structure of oxytocin is very similar to that of vasopressin. Oxytocin and vasopressin were discovered, isolated and synthesized by Vincent du Vigneaud in 1953, work for which he received the Nobel Prize in Chemistry in 1955.
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Oxytocin is a peptide of nine different amino acids: cysteine, tyrosine, isoleucine, glutamine, asparagines, cysteine, praline, leucine, glycine (abbreviated CYIQNCPLG). It is almost identical to vasopressin, with the single difference being that vasopressin has argine or lysine in the position of leucine. Oxytocin is often found bound to neurophysin, a carrier protein.
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Oxytocin, vasopressin, and vasotocin each caused dose-dependent increases in [3H]IPtotal in T3–1 cells labeled with [3H]inositol and then stimulated in the presence of 10 mM LiCl (Fig. 1). These effects were... relatively modest compared with the 15-fold increase caused by GnRH, with maximal concentrations approximately doubling basal levels of [3H]IPtotal accumulation. Although there was a tendency for vasopressin to have greater efficacy than oxytocin (which might reflect simultaneous activation by vasopressin of both oxytocin and vasopressin-selective receptors), it was not statistically significant (P > 0.1). However oxytocin was the most potent of these peptides (EC50 0.1 nM), indicating that the effects observed are mediated predominantly or solely by oxytocin-selective receptors.
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