期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1980
卷号：77
期号：7
页码：3947-3951
DOI：10.1073/pnas.77.7.3947
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
