Complete amino acid sequence of mouse prolactin.
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.
D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D004590:Electrophoresis, Paper; D006801:Humans; D051379:Mice; D010446:Peptide Fragments / Q000302:isolation & purification; D011388:Prolactin; D051381:Rats; D012756:Sheep; D013045:Species Specificity; D013552:Swine
D010446:Peptide Fragments; D011388:Prolactin