Simpson R J, Moritz R L, Lloyd C J, Fabri L J, Nice E C, Rubira M R, Burgess A W
Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research (Melbourne), Victoria, Australia.
FEBS Lett. 1987 Nov 16;224(1):128-32. doi: 10.1016/0014-5793(87)80435-0.
The complete amino acid sequence of basic FGF (146 residues) from ovine pituitary glands has been established. This has been achieved by the sequence analysis of subnanomole amounts of the intact molecule and of peptides derived by enzymatic digestions with clostripain, chymotrypsin, pepsin and Staphylococcus aureus V8 protease. Microbore HPLC, employing 1-2 mm i.d. columns, was used to purify, concentrate and buffer-exchange the FGF peptides. A novel application of ion-pairing chromatography was employed to isolate peptides which were not retained on conventional reversed-phase systems. There is only one positional difference between the ovine and bovine basic FGFs, but there are 3 positional differences between ovine and human basic FGFS.
已确定来自绵羊垂体的碱性成纤维细胞生长因子(146个残基)的完整氨基酸序列。这是通过对亚纳摩尔量的完整分子以及用梭菌蛋白酶、胰凝乳蛋白酶、胃蛋白酶和金黄色葡萄球菌V8蛋白酶进行酶切得到的肽段进行序列分析实现的。使用内径为1 - 2毫米的微径高效液相色谱来纯化、浓缩和进行碱性成纤维细胞生长因子肽段的缓冲液置换。采用离子对色谱的一种新应用来分离在传统反相系统上不保留的肽段。绵羊和牛的碱性成纤维细胞生长因子之间只有一个位置差异,但绵羊和人的碱性成纤维细胞生长因子之间有3个位置差异。