Eastgate J A, Symons J A, Duff G W
University of Edinburgh Department of Medicine, RDU, Northern General Hospital, Scotland.
FEBS Lett. 1990 Jan 29;260(2):213-6. doi: 10.1016/0014-5793(90)80106-s.
A covalent cross-linking technique was used to bind iodinated interleukin-1 (IL1) alpha and beta to plasma proteins. One specific IL1 beta binding protein was observed, that when cross-linked to 125I-IL1 beta migrated to approximately 60 kDa on SDS-PAGE. The protein did not bind IL1 alpha. The 43 -kDa protein was partially purified using a wheat germ agglutinin affinity column. The isolated factor again specifically bound IL1 beta, and appeared to consist of single chain glycoprotein. The protein was heat stable and had a rapid association time with IL1 beta. This protein may be an important carrier molecule for IL1 beta in vivo.
采用共价交联技术将碘化白细胞介素-1(IL1)α和β与血浆蛋白结合。观察到一种特异性的IL1β结合蛋白,当它与125I-IL1β交联后,在SDS-PAGE上迁移至约60 kDa处。该蛋白不结合IL1α。利用麦胚凝集素亲和柱对43 kDa的蛋白进行了部分纯化。分离得到的因子再次特异性结合IL1β,且似乎由单链糖蛋白组成。该蛋白热稳定,与IL1β的结合时间较快。这种蛋白可能是体内IL1β的一种重要载体分子。