Conlon J M, O'Harte F, Peter R E, Kah O
Department of Biomedical Sciences, Creighton University Medical School, Omaha, Nebraska 68178.
J Neurochem. 1991 Apr;56(4):1432-6. doi: 10.1111/j.1471-4159.1991.tb11442.x.
A 21-amino-acid residue tachykinin-related peptide, carassin, was isolated in pure form from an extract of the brain of the goldfish, Carrassius auratus, by reversed-phase HPLC. The primary structure of the peptide was established as the following: Ser-Pro-Ala-Asn-Ala-Gln-Ile-Thr-Arg-Lys-Arg-His-Lys-Ile-Asn- Ser-Phe-Val-Gly-Leu-Met.NH2. This amino acid sequence is the same length as and shows structural similarity (57% homology) to the mammalian tachykinin, neuropeptide-gamma, which is a product of the posttranslational processing of gamma-preprotachykinin. The mammalian tachykinins, substance P and neurokinin B, were not detected in the extract by using specific antisera directed against the NH2-termini of the peptides, but an antiserum directed against the COOH-terminal region of substance P did detect a low concentration of immunoreactive material.
一种由21个氨基酸残基组成的速激肽相关肽——鲫鱼速激肽,通过反相高效液相色谱法从金鱼(Carassius auratus)脑提取物中以纯形式分离出来。该肽的一级结构确定如下:Ser-Pro-Ala-Asn-Ala-Gln-Ile-Thr-Arg-Lys-Arg-His-Lys-Ile-Asn-Ser-Phe-Val-Gly-Leu-Met.NH2。此氨基酸序列与哺乳动物速激肽神经肽γ长度相同且显示出结构相似性(57%同源性),神经肽γ是γ-前速激肽原翻译后加工的产物。利用针对肽NH2末端的特异性抗血清在提取物中未检测到哺乳动物速激肽P物质和神经激肽B,但针对P物质COOH末端区域的抗血清确实检测到了低浓度的免疫反应性物质。