ISOLATION AND PRIMARY STRUCTURE OF NEUROPEPTIDES FROM THE MOSQUITO, AEDES-AEGYPTI, IMMUNOREACTIVE TO FMRFAMIDE ANTISERUM
ISOLATION AND PRIMARY STRUCTURE OF NEUROPEPTIDES FROM THE MOSQUITO, AEDES-AEGYPTI, IMMUNOREACTIVE TO FMRFAMIDE ANTISERUM
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DOI：
10.1016/0020-1790(89)90073-5
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发表时间：
1989-01-01
期刊：
影响因子：
--
通讯作者：
LEA, AO
中科院分区：
文献类型：
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作者：
MATSUMOTO, S;BROWN, MR;LEA, AO
两种新的神经肽，Aea-HP-I和II，已被分离出的头部提取物的蚊子，埃及伊蚊，它们被检测到的FMRFamide放射免疫测定。通过凝胶过滤、离子交换色谱和反相高效液相色谱对肽进行纯化。氨基酸组成和序列分析结合酶切，确定Aea-HP-I的一级结构为pGlu-Arg-Pro-Hyp-Ser-Leu-Lys-Thr-Arg-Phe-NH 2，Aea-HP-II的一级结构为Thr-Arg-Phe-NH 2。合成了Aea-HP-I，合成肽的色谱性质与天然肽的色谱性质相同，从而证实了结构分析。该肽有三个不寻常的残基：氨基末端的pGlu，第四位的Hyp和羧基末端的酰胺。Pro-Hyp序列存在于锥螺和黄蜂毒液的毒素肽和缓激肽类似物中。虽然Aea-HP-I和II的功能尚未确定，但这些肽在羧基末端具有与蟑螂中的Lem-SK-I和II（白细胞磺胺激肽）和Lem-MS（白细胞肌抑制素）以及软体动物中的FMRFamide相关肽相同的RFa序列。
Two novel neuropeptides, Aea-HP-I and II, have been isolated from a head extract of the mosquito, Aedes aegypti; they were detected by a FMRFamide radioimmunoassay. The peptides were purified by gel filtration, ion exchange chromatography, and reversed-phase high performance liquid chromatography. Amino acid composition and sequence analysis, combined with enzymatic digestion, established the primary structure of Aea-HP-I as pGlu-Arg-Pro-Hyp-Ser-Leu-Lys-Thr-Arg-Phe-NH2 and Aea-HP-II as Thr-Arg-Phe-NH2. Aea-HP-I was synthesized, and chromatographic properties of the synthetic peptide were the same as those of the native peptide, thus confirming the structural analysis. The peptide has three unusual residues: an amino-terminal pGlu, a Hyp in the fourth position, and a carboxyl-terminal amide. The Pro-Hyp sequence occurs in toxin peptides from the venoms of cone snails and wasps and in bradykinin analogues. Although the functions of Aea-HP-I and II have not been determined, the peptides have the same RFa sequence at the carboxyl-terminal as Lem-SK-I and II (leucosulfakinins) and Lem-MS (leucomyosuppressin) in cockroaches and FMRFamide-related peptides in molluscs.