Lowry P J, Bennett H P, McMartin C
Biochem J. 1974 Aug;141(2):427-37. doi: 10.1042/bj1410427.
An adrenocorticotrophic hormone (ACTH) was isolated from extracts of the pars distalis of the pituitary of the dogfish Squalus acanthias by gel filtration and ion-exchange chromatography. It had 15% of the potency of human ACTH in promoting cortico-steroidogenesis in isolated rat adrenal cells. Sequence analysis revealed it to be a nonatria-contapeptide with the following primary structure: Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Met-Gly-Arg-Lys-Arg-Arg-Pro-Ile-Lys-Val-Tyr-Pro-Asn-Ser-Phe-Glu-Asp-Glu-Ser-Val-Glu-Asn-Met-Gly-Pro-Glu-Leu. The N-terminal tridecapeptide sequence was identical with the proposed structure of dogfish alpha-melanocyte-stimulating hormone (alpha-MSH). On comparison with human ACTH eleven amino acid differences were seen, nine of which are in the 20-39 region of the molecule which is not essential for the steroidogenic activity of ACTH. A peptide identical with the 18-39 portion of this new ACTH was similarly isolated from the neurointermediate lobe of the pituitary where considerable amounts of dogfish alpha-MSH were found. This supported our view that ACTH as well as having a distinct biological role of its own is also the precursor of alpha-MSH.
通过凝胶过滤和离子交换色谱法，从角鲨（Squalus acanthias）垂体远侧部提取物中分离出一种促肾上腺皮质激素（ACTH）。在促进分离的大鼠肾上腺细胞皮质类固醇生成方面，它的效力是人类ACTH的15%。序列分析表明它是一种九肽促肾上腺皮质激素，其一级结构如下：Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Met-Gly-Arg-Lys-Arg-Arg-Pro-Ile-Lys-Val-Tyr-Pro-Asn-Ser-Phe-Glu-Asp-Glu-Ser-Val-Glu-Asn-Met-Gly-Pro-Glu-Leu。其N端十三肽序列与角鲨α-黑素细胞刺激素（α-MSH）的推测结构相同。与人类ACTH相比，发现有11个氨基酸差异，其中9个位于分子的20-39区域，该区域对ACTH的类固醇生成活性并非必需。从垂体神经中间叶中同样分离出一种与这种新ACTH的18-39部分相同的肽，在该神经中间叶中发现了大量角鲨α-MSH。这支持了我们的观点，即ACTH不仅具有自身独特的生物学作用，也是α-MSH的前体。
