Complete amino acid sequence of mouse prolactin
Open Access
- 1 January 1984
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 138 (2) , 227-237
- https://doi.org/10.1111/j.1432-1033.1984.tb07905.x
Abstract
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.This publication has 48 references indexed in Scilit:
- Conformational studies of secreted mouse pituitary prolactinBiochemistry, 1982
- SECONDARY STRUCTURE PREDICTION OF ANTERIOR PITUITARY HORMONES Lack of Correlation between Predicted Values and Circular Dichroism DataInternational Journal of Peptide and Protein Research, 1979
- Empirical Predictions of Protein ConformationAnnual Review of Biochemistry, 1978
- Nucleotide sequence and amplification in bacteria of structural gene for rat growth hormoneNature, 1977
- Primary structure of α‐subunit of DNA‐dependent RNA polymerase from Escherichia coliFEBS Letters, 1977
- The primary structure of bovine prolactinFEBS Letters, 1974
- Solid‐phase edman degradation: Attachment of carboxyl‐terminal homoserine peptides to an insoluble resinFEBS Letters, 1973
- The primary structure of bovine growth hormoneFEBS Letters, 1973
- Selective modification of tryptophan-149 in ovine pituitary lactogenic hormoneBiochemistry, 1973
- Logical analysis of the mechanism of protein folding: I. Predictions of helices, loops and β-structures from primary structureJournal of Molecular Biology, 1973