Kirsch T, Nickel J, Sebald W
Physiologische Chemie II, Biozentrum der Universität Würzburg, Am Hubland, D-97074, Würzburg, Germany.
FEBS Lett. 2000 Feb 25;468(2-3):215-9. doi: 10.1016/s0014-5793(00)01214-x.
Bone morphogenetic protein-2 (BMP-2) is a member of the transforming growth factor beta superfamily which induces bone formation and regeneration, and important steps during early embryonic development. BMP-2 signals via oligomerization of type I and type II serine/threonine kinase receptors. We report here expression of the extracellular domain of the human type IA receptor for BMP-2 (BMPR-IA) in Escherichia coli. This soluble form of BMPR-IA (sBMPR-IA) was purified employing a BMP-2 affinity column. Gel filtration experiments and analysis of gel filtration fractions by polyacrylamide electrophoresis and densitometry reveal that BMP-2 forms a defined 1:2 complex with sBMPR-IA that can be purified and hopefully used for crystallization studies.
骨形态发生蛋白-2（BMP-2）是转化生长因子β超家族的成员，可诱导骨形成和再生，也是早期胚胎发育过程中的重要步骤。BMP-2通过I型和II型丝氨酸/苏氨酸激酶受体的寡聚化来传递信号。我们在此报告人BMP-2的IA型受体（BMPR-IA）细胞外结构域在大肠杆菌中的表达。这种可溶性形式的BMPR-IA（sBMPR-IA）通过BMP-2亲和柱进行纯化。凝胶过滤实验以及通过聚丙烯酰胺电泳和光密度测定法对凝胶过滤级分的分析表明，BMP-2与sBMPR-IA形成了确定的1:2复合物，该复合物可以被纯化，并有望用于结晶研究。
