Denis D, Day R, Lemaire S
Int J Pept Protein Res. 1982 Jan;19(1):18-24.
Two highly potent dynorphin-like peptides were isolated from bovine adrenal medulla by successive chromatography of an acid (HCl) extract on Sephadex G-10, carboxymethylcellulose, Sephadex G-50 and partition chromatography on Sephadex G-50. Amino acid analysis of both peptides revealed the presence of 24 amino acids including the composition of dynorphin-(1-13) and differing from each other only by a few residues. Both peptides were shown to have the same activity as dynorphin-(1-13) in the guniea pig ileum assay and reacted as well as dynorphin-(1-13) with a specific antibody (R-31) directed against the synthetic material.
通过对牛肾上腺髓质的酸（HCl）提取物先后进行Sephadex G - 10、羧甲基纤维素、Sephadex G - 50柱层析以及Sephadex G - 50分配层析，从牛肾上腺髓质中分离出了两种高效能的强啡肽样肽。对这两种肽的氨基酸分析表明，它们含有24种氨基酸，包括强啡肽 -（1 - 13）的组成，彼此之间仅相差几个残基。在豚鼠回肠试验中，这两种肽均显示出与强啡肽 -（1 - 13）相同的活性，并且与针对合成材料的特异性抗体（R - 31）反应情况也与强啡肽 -（1 - 13）相同。
