Answers are grounded in this paper and cite their sources.
The complete primary structure of mouse prolactin has been established on the basis of tryptic peptides from cyanogen-bromide-treated, S-carboxymethylated mouse prolactin and Staphylococcus-aureus-protease-cleaved overlaps, which were sequenced by manual liquid-phase and solid-phase Edman degradation. Three disulfide bonds were assigned to Cys-4-Cys-9, Cys-56-Cys-172, and Cys-189-Cys-197 by digestion of intact prolactin with S. aureus protease. One of the characteristics to date is replacement of Trp-89, which is commonly present among prolactin, growth hormone and choriomammotropin, by serine. It was suggested, by comparison with five other prolactins, five growth hormones and human choriomammotropin, that Asp-18, His-25, Ser-60 and Thr-63 are essential to lactogenic activity.
No takes yet. Share an insight, caveat, or question.
Kohmoto et al. (1984) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: