Phares G A, Walent J H, Niece R L, Kumar S B, Ericsson L H, Kowalak J A, Lloyd P E
Committee on Neurobiology, University of Chicago, Illinois 60637, USA.
Biochemistry. 1996 May 7;35(18):5921-7. doi: 10.1021/bi953081y.
We report the purification and characterization of a novel neuropeptide from Aplysia nervous tissue. The peptide was termed cerebral peptide 2 (CP2) because it was the larger of two peptides predominantly synthesized in the cerebral ganglia and transported to other regions of the central nervous system. The purification of CP2 from extracts of cerebral ganglia using three sequential modes of high-pressure liquid chromatography (HPLC) was followed using the [35S]methionine-labeled peptide obtained from transport experiments. The primary structure of CP2 was determined by automated Edman degradation of native CP2 and its proteolytic fragments in conjunction with mass spectrometry. CP2 is a 41 amino acid peptide with an amidated carboxyl terminal. A peptide with the proposed sequence of CP2 was synthetized and compared by HPLC with the native peptide. Chromatographic properties of the synthetic and native peptide labeled in vivo were found to be identical. CP2 does not appear to be a member of any previously identified peptide family.
我们报道了从海兔神经组织中纯化和鉴定一种新型神经肽的过程。该肽被命名为脑肽2（CP2），因为它是主要在脑神经节中合成并运输到中枢神经系统其他区域的两种肽中较大的一种。使用[35S]甲硫氨酸标记的肽进行运输实验，随后通过三种连续的高压液相色谱（HPLC）模式从脑神经节提取物中纯化CP2。CP2的一级结构通过对天然CP2及其蛋白水解片段进行自动Edman降解并结合质谱法来确定。CP2是一种含有41个氨基酸且羧基末端酰胺化的肽。合成了具有CP2提议序列的肽，并通过HPLC与天然肽进行比较。发现体内标记的合成肽和天然肽的色谱特性相同。CP2似乎不属于任何先前鉴定的肽家族。
