Heulin M H, Rajoelina J, Artur M, Geschier C, Straczek J, Lasbennes A, Belleville F, Nabet P
Life Sci. 1987 Jul 20;41(3):297-304. doi: 10.1016/0024-3205(87)90152-4.
A low molecular weight growth factor (LMW-GF) enriched preparation was purified from human plasma after ultrafiltration or gel filtration by means of molecular sieving chromatography low pressure reversed phase chromatography (LP-RPLC) and electrophoresis. Purification was monitored by a biological assay testing the capacity of the fractions to enhance the sulfation activity of the somatomedins/insulin-like growth factors on chick embryo cartilage. Analysis of its chemical nature show that it is hydrophilic, stable to heat, resistant to most of the proteases but that it is degraded by acid hydrolysis or carboxypeptidase Y action. UV absorption spectrum and ion-exchange chromatographic retention behavior support the hypothesis that the most purified active preparation includes a peptide structure. The presence of sugar is suggested by concanavalin A binding experiments. The fact that the purification fractions also enhance thymidine uptake by other cell lines (fibroblasts, activated lymphocytes) widens the role of such small plasma molecules in the field of growth factor activities.
通过超滤或凝胶过滤，借助分子筛分色谱、低压反相色谱（LP-RPLC）和电泳，从人血浆中纯化出一种富含低分子量生长因子（LMW-GF）的制剂。通过生物测定法监测纯化过程，该测定法检测各组分增强生长调节素/胰岛素样生长因子对鸡胚软骨硫酸化活性的能力。对其化学性质的分析表明，它具有亲水性，对热稳定，对大多数蛋白酶具有抗性，但会被酸水解或羧肽酶Y作用降解。紫外吸收光谱和离子交换色谱保留行为支持这样的假设，即最纯的活性制剂包含肽结构。伴刀豆球蛋白A结合实验表明存在糖类。纯化组分还能增强其他细胞系（成纤维细胞、活化淋巴细胞）对胸腺嘧啶核苷的摄取，这一事实拓宽了此类小血浆分子在生长因子活性领域的作用。
