Yashima T, Tsuchiya A, Morita O, Terabe S
Pharmaceutical Research Laboratories, Kyowa Hakko Kogyo Company, Ltd., Shizuoka, Japan.
Anal Chem. 1992 Dec 1;64(23):2981-4. doi: 10.1021/ac00047a018.
Large peptides with similar electrophoretic mobilities were separated by micellar electrokinetic chromatography (MEKC) with organic modifiers. [Leu13]motilin and [Met13]motilin differ by only one neutral amino acid residue. Because the electrophoretic mobilities of these peptides are almost identical, these peptides were not separated by capillary zone electrophoresis (CZE). Such large peptides have not been separated by conventional MEKC either, because they interacted strongly with the micelle. However, they were completely separated by MEKC when an organic solvent was added to the micellar solution. Some insulins, larger peptides than motilin, from different origins, which have very similar electrophoretic mobilities, were also successfully separated by the same technique. The size of peptides which were separated without organic modifiers was examined.
通过含有有机改性剂的胶束电动色谱法(MEKC)分离了具有相似电泳迁移率的大肽。[亮氨酸13]胃动素和[甲硫氨酸13]胃动素仅相差一个中性氨基酸残基。由于这些肽的电泳迁移率几乎相同,因此它们不能通过毛细管区带电泳(CZE)分离。这类大肽也不能通过传统的MEKC分离,因为它们与胶束强烈相互作用。然而,当向胶束溶液中加入有机溶剂时,它们通过MEKC被完全分离。一些来源不同、电泳迁移率非常相似、比胃动素更大的胰岛素肽也通过相同技术成功分离。研究了在不使用有机改性剂的情况下分离得到的肽的大小。