Imamura T, Tokita Y, Mitsui Y
Cell Science and Technology Division, Fermentation Research Institute, Tsukuba Science City, Japan.
Biochem Biophys Res Commun. 1988 Sep 15;155(2):583-90. doi: 10.1016/s0006-291x(88)80534-5.
Receptor molecules for basic fibroblast growth factor (bFGF) were isolated from rat brain by a novel and rapid procedure and characterized. Purification was performed by wheatgerm agglutinin (WGA) gel affinity chromatography in combination with bFGF gel affinity chromatography, utilizing a novel elution method involving heparin. The eluted proteins were active in binding bFGF and were separated as two bands with respective molecular masses of 140 kDa and 110 kDa on SDS-PAGE. More than half of this bFGF-binding activity was lost after 16 h at 4 degrees C. Thus, bFGF receptors were purified as labile glycoconjugates.
通过一种新颖快速的方法从大鼠脑中分离并鉴定了碱性成纤维细胞生长因子（bFGF）的受体分子。纯化过程采用麦胚凝集素（WGA）凝胶亲和层析结合bFGF凝胶亲和层析，并运用一种涉及肝素的新型洗脱方法。洗脱的蛋白质具有结合bFGF的活性，在SDS-PAGE上分离为两条带，分子量分别为140 kDa和110 kDa。在4℃下放置16小时后，这种bFGF结合活性丧失了一半以上。因此，bFGF受体被纯化为不稳定的糖缀合物。
