Bennett H P, Seidah N G, Benjannet S, Solomon S, Chrétien M
Int J Pept Protein Res. 1986 Mar;27(3):306-13. doi: 10.1111/j.1399-3011.1986.tb01825.x.
The cystine bridge structure of the amino-terminal fragment of human pro-opiomelanocortin has been reinvestigated. Highly purified amino-terminal fragment 1-76 was rapidly isolated from human pituitaries using only reverse-phase liquid chromatography (RP-HPLC). This peptide was then subjected to trypsin and V8-protease digestion and the products separated by RP-HPLC and subjected to amino acid and microsequence analysis. The results show that disulfide bridges link Cys-2 to Cys-24 and Cys-8 to Cys-20. Amino acid analysis and amino sugar determination confirm (i) the previously proposed sequence and (ii) the suggestion of the presence of two glycosylation sites in this molecule. These are most probably located at Thr-45 (O-glycosylation) and at Asn-65 (N-glycosylation).
人促阿片黑素细胞皮质素氨基末端片段的胱氨酸桥结构已被重新研究。仅使用反相液相色谱法（RP-HPLC）就从人垂体中快速分离出了高度纯化的1-76氨基末端片段。然后将该肽用胰蛋白酶和V8蛋白酶消化，产物通过RP-HPLC分离，并进行氨基酸和微序列分析。结果表明，二硫键将半胱氨酸-2与半胱氨酸-24以及半胱氨酸-8与半胱氨酸-20相连。氨基酸分析和氨基糖测定证实了（i）先前提出的序列，以及（ii）该分子中存在两个糖基化位点的推测。这些位点很可能位于苏氨酸-45（O-糖基化）和天冬酰胺-65（N-糖基化）处。
