Li Q G, Blacher R, Esch F, Congote L F
Endocrine Laboratory, Royal Victoria Hospital, Montreal, Canada.
Biochem Biophys Res Commun. 1990 Jan 30;166(2):557-61. doi: 10.1016/0006-291x(90)90844-d.
An 8 kd heparin-binding peptide which stimulates thymidine incorporation in cultures of fetal calf liver erythroid cells was isolated from fetal bovine serum by affinity chromatography on Heparin-Sepharose, ion exchange chromatography, gel filtration and reversed-phase HPLC. The N-terminal sequence of the isolated peptide was identical to the N-terminal sequence of bovine erythrotropin or insulin-like growth factor II (IGF II). The potential heparin-binding site of IGF II is probably situated in the arginine-rich C-peptide region. The affinities of human recombinant IGF I and II were compared with those of apolipoprotein H (a plasma heparin-binding protein) and bovine insulin in a heparin-affinity column. The retention times were in the order: Apolipoprotein H greater than hrIGF II greater than hrIGF I greater than insulin (no retention). This unusual property of IGF II suggests that it may be captured in the extracellular matrix in a similar way to fibroblast growth factor, interleukin 3 or granulocyte/macrophage colony-stimulating factor.
通过肝素-琼脂糖亲和色谱、离子交换色谱、凝胶过滤和反相高效液相色谱从胎牛血清中分离出一种8kd的肝素结合肽，该肽可刺激胎牛肝红系细胞培养物中的胸腺嘧啶掺入。分离出的肽的N端序列与牛促红细胞生成素或胰岛素样生长因子II（IGF II）的N端序列相同。IGF II的潜在肝素结合位点可能位于富含精氨酸的C肽区域。在肝素亲和柱中比较了重组人IGF I和II与载脂蛋白H（一种血浆肝素结合蛋白）和牛胰岛素的亲和力。保留时间顺序为：载脂蛋白H＞hrIGF II＞hrIGF I＞胰岛素（无保留）。IGF II的这种不寻常特性表明，它可能以与成纤维细胞生长因子、白细胞介素3或粒细胞/巨噬细胞集落刺激因子类似的方式被捕获在细胞外基质中。
