Oumi T, Ukena K, Matsushima O, Ikeda T, Fujita T, Minakata H, Nomoto K
Faculty of Science, Hiroshima University, Japan.
Biochem Biophys Res Commun. 1995 Nov 22;216(3):1072-8. doi: 10.1006/bbrc.1995.2730.
Three novel bioactive peptides, which were structurally related to each other, were purified and chemically identified from two species of the earthworms, Eisenia foetida and Pheretima vittata. One peptide was isolated from the gut tissue of E. foetida, and the other two were purified from the whole body of E. foetida and P. vittata, respectively. These peptides consisted of 17 or 18 amino acid residues and were named GGNG peptides after their unique, common structure of the C-termini. These GGNG peptides augmented both tension and frequency of spontaneous contractions of isolated gut preparations of E. foetida, and also elicited contractions of other annelidan tissues such as the polychaete esophagus and the leech vagina. However, they showed no activity on molluscan or arthropodan tissues, suggesting that GGNG peptides may be peculiar to annelids. No peptides homologous to GGNG peptides have been known so far in any living organisms.
从两种蚯蚓，即赤子爱胜蚓（Eisenia foetida）和威廉腔环蚓（Pheretima vittata）中纯化并化学鉴定出三种结构相关的新型生物活性肽。一种肽是从赤子爱胜蚓的肠道组织中分离出来的，另外两种分别从赤子爱胜蚓和威廉腔环蚓的整体中纯化得到。这些肽由17或18个氨基酸残基组成，因其C端独特的共同结构而被命名为GGNG肽。这些GGNG肽增强了赤子爱胜蚓离体肠道制剂的张力和自发收缩频率，还能引发其他环节动物组织的收缩，如多毛纲动物的食管和水蛭的阴道。然而，它们对软体动物或节肢动物组织没有活性，这表明GGNG肽可能是环节动物所特有的。迄今为止，在任何生物体中都尚未发现与GGNG肽同源的肽。
