Open AccessIsolation, structure, biological characterization, and synthesis of beta-[Tyr9]melanotropin-(9-18) decapeptide from pig hypothalami.
Author(s) -
Andrew V. Schally,
Robert C. Chang,
Wei Huang,
David H. Coy,
Abba J. Kastin,
Tommie W. Redding
Publication year - 1980
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.7.3947
Subject(s) - tetrapeptide , tyrosine , chemistry , amino acid , residue (chemistry) , prohormone , peptide sequence , histidine , peptide , stereochemistry , biochemistry , oligopeptide , biological activity , beta (programming language) , hormone , in vitro , gene , computer science , programming language
A decapeptide with the amino acid sequence H-Tyr-Phe-Arg-Trp-Gly-Ser-Pro-Pro-Lys-Asp-OH was isolated from acid extracts of porcine hypothalami, structurally and biologically characterized, and synthesized. Except for the NH2-terminal tyrosine, this decapeptide corresponds to the amino acid sequences 9-18 of porcine beta-melanotropin (beta-MSH) and 49-58 of porcine beta-lipotropin (beta-LPH); it also has a tetrapeptide sequence of amino acids (Phe-Arg-Trp-Gly) common to the 7-10 sequences in corticotropin (ACTH) and alpha-MSH. beta-MSH, beta-LPH, alphaMSH, and ACTH from various species all have a histidine residue in the position immediately preceding the common sequence, and the occurrence of a natural peptide with the tyrosine residue in the corresponding site has not been previously reported. This suggests that the beta-[Tyr9]MSH-(9-18) decapeptide might be a fragment of a still larger precursor (prohormone) possibly related to beta-LPH.