Gäde G, Hilbich C, Beyreuther K, Rinehart K L
Institut für Zoologie IV, Universität Düsseldorf, F.R.G.
Peptides. 1988 Jul-Aug;9(4):681-8. doi: 10.1016/0196-9781(88)90107-6.
Two neuropeptides with adipokinetic activity in Locusta migratoria and hypertrehalosaemic activity in Periplaneta americana were purified by high-performance liquid chromatography from the corpus cardiacum of the lubber grasshopper, Romalea microptera. The sequences of both peptides, designated Ro I and Ro II, were determined by gas-phase sequencing employing Edman degradation after the N-terminal pyroglutamate residue was enzymatically deblocked, as well as by fast atom bombardment mass spectrometry. Ro I was found to be a decapeptide with the primary structure: pGlu-Val-Asn-Phe-Thr-Pro-Asn-Trp-Gly-Thr-NH2, whereas Ro II is an octapeptide with the structure: pGlu-Val-Asn-Phe-Ser-Thr-Gly-Trp-NH2. Ro II is identical with AKH-G isolated from the cricket Gryllus bimaculatus. Synthetic materials having the assigned structures were found to be chromatographically, mass spectrometrically, and biologically indistinguishable from the natural peptides, confirming the sequences and establishing the Romalea peptides as members of the AKH/RPCH-family of peptides.
从美洲大蠊的心脏体中,通过高效液相色谱法从巨型蝗虫Romalea microptera的心脏体中纯化出两种具有脂肪动力活性(在飞蝗中)和高海藻糖血症活性(在美洲大蠊中)的神经肽。这两种肽分别命名为Ro I和Ro II,其序列通过在N端焦谷氨酸残基经酶解去封闭后采用埃德曼降解的气相测序法以及快原子轰击质谱法确定。发现Ro I是一种十肽,其一级结构为:pGlu-Val-Asn-Phe-Thr-Pro-Asn-Trp-Gly-Thr-NH2,而Ro II是一种八肽,结构为:pGlu-Val-Asn-Phe-Ser-Thr-Gly-Trp-NH2。Ro II与从双斑蟋蟀Gryllus bimaculatus中分离出的AKH-G相同。发现具有指定结构的合成材料在色谱、质谱和生物学性质上与天然肽无法区分,从而确认了序列,并确定Romalea肽为AKH/RPCH肽家族的成员。