Potts J T, Tregear G W, Keutmann H T, Niall H D, Sauer R, Deftos L J, Dawson B F, Hogan M L, Aurbach G D
Proc Natl Acad Sci U S A. 1971 Jan;68(1):63-7. doi: 10.1073/pnas.68.1.63.
Determination of the amino acid sequence of bovine parathyroid hormone has led to the synthesis of a tetratriacontapeptide corresponding to the amino-terminal 1-34 residues of the native molecule. The specific biological effects of this synthetic peptide on bone and kidney are qualitatively identical to those of the native hormone in classical bioassays in vivo and in several systems in vitro. Potency of the synthetic peptide equals or exceeds that of a biologically active fragment of comparable size isolated from the native hormone; the synthetic and natural peptides show complete immunological cross-reactivity. Thus, essential requirements for the physiological actions of the peptide on both skeletal and renal tissue are contained within the 34 amino-terminal amino acids. The potency of the synthetic peptide, relative to that of the native (84-amino acid) polypeptide, is greater in vitro than in vivo; this suggests that the carboxyl terminal two-thirds of the native hormone may protect the circulating polypeptide from rapid metabolic degradation.
牛甲状旁腺激素氨基酸序列的确定，已促成了一种三十四肽的合成，该三十四肽对应于天然分子的氨基末端1 - 34个残基。在体内经典生物测定以及多个体外系统中，这种合成肽对骨骼和肾脏的特定生物学效应在性质上与天然激素相同。合成肽的效力等于或超过从天然激素中分离出的大小相当的生物活性片段；合成肽和天然肽显示出完全的免疫交叉反应性。因此，该肽对骨骼和肾脏组织生理作用的基本要求包含在34个氨基末端氨基酸内。相对于天然（84个氨基酸）多肽，合成肽在体外的效力比在体内更大；这表明天然激素羧基末端的三分之二可能保护循环中的多肽免于快速代谢降解。
