Milton R C, Mayer E, Walsh J H, Rivier J E, Dykert J, Lee T D, Shively J E, Reeve J R
Peptide Biology Laboratory, Salk Institute, La Jolla, California.
Int J Pept Protein Res. 1988 Aug;32(2):141-52. doi: 10.1111/j.1399-3011.1988.tb00674.x.
Two canine gastrin-releasing peptides originally isolated from gut tissue extracts have been synthesized by solid phase methodology and purified by preparative reverse phase high performance liquid chromatography (RP-HPLC). The synthetic gastrin-releasing peptides GRP1-27 and GRP 5-27 were characterized with regard to homogeneity and composition using nine different RP-HPLC systems, mass spectroscopy, amino acid analysis, Edman degradation, methionine oxidation, and peptide mapping with tryptic, Staph. aureus V8 protease and cyanogen bromide cleavage (the latter two systems performed only with GRP 1-27). Although a scarcity of the natural products prevented quantitative biological comparison of the synthetic and natural peptides, they were found to elute identically on RP-HPLC co-chromatography and similar dose dependent biological potencies were observed in canine antral muscle tissue contraction experiments. Indeed, all the peptides containing the bombesin-like carboxyl terminal decapeptide sequence studied to date have similar biological activities.
最初从肠道组织提取物中分离出的两种犬胃泌素释放肽已通过固相方法合成，并通过制备型反相高效液相色谱（RP-HPLC）进行纯化。使用九种不同的RP-HPLC系统、质谱、氨基酸分析、埃德曼降解、甲硫氨酸氧化以及用胰蛋白酶、金黄色葡萄球菌V8蛋白酶和溴化氰裂解进行肽图谱分析（后两种系统仅对GRP 1-27进行），对合成的胃泌素释放肽GRP1-27和GRP 5-27的均一性和组成进行了表征。尽管天然产物的稀缺性使得无法对合成肽和天然肽进行定量生物学比较，但发现它们在RP-HPLC共色谱上的洗脱行为相同，并且在犬胃窦肌组织收缩实验中观察到了相似的剂量依赖性生物学活性。事实上，迄今为止研究的所有含有蛙皮素样羧基末端十肽序列的肽都具有相似的生物学活性。
