Kohmoto K, Tsunasawa S, Sakiyama F
Eur J Biochem. 1984 Jan 16;138(2):227-37. doi: 10.1111/j.1432-1033.1984.tb07905.x.
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.
