van Heusden M C, Fogarty S, Porath J, Law J H
Department of Biochemistry, Biological Sciences West, University of Arizona, Tucson 85721.
Protein Expr Purif. 1991 Feb;2(1):24-8. doi: 10.1016/1046-5928(91)90004-3.
Vitellogenin and vitellin of Manduca sexta and some other insect species were purified by immobilized metal ion affinity chromatography. Ferric ion was chosen as the immobilized metal ion. Agarose-bound carboxymethylpicolylamine was used as the chelating adsorbent for the ferric ion. Vitellogenin and vitellin, both phosphorylated lipoproteins, were shown to bind specifically to the iron. The general applicability of immobilized ferric ion affinity chromatography for the purification of insect vitellogenin and vitellin is suggested.
通过固定化金属离子亲和色谱法纯化了烟草天蛾及其他一些昆虫物种的卵黄原蛋白和卵黄磷蛋白。选择铁离子作为固定化金属离子。琼脂糖结合的羧甲基吡啶胺用作铁离子的螯合吸附剂。卵黄原蛋白和卵黄磷蛋白这两种磷酸化脂蛋白均显示出能与铁特异性结合。这表明固定化铁离子亲和色谱法在纯化昆虫卵黄原蛋白和卵黄磷蛋白方面具有普遍适用性。
