Flynn G, Joly J C, Purich D L
Department of Biochemistry and Molecular Biology, University of Florida College of Medicine, Gainesville 32610.
Biochem Biophys Res Commun. 1987 Nov 13;148(3):1453-9. doi: 10.1016/s0006-291x(87)80295-4.
We have developed a thrombin proteolytic cleavage procedure to obtain higher yields of the Mr 28,000 microtubule-binding and Mr 240,000 microtubule-projection components of MAP-2. The former is a highly basic component, whereas the latter and intact MAP-2 are acidic polypeptides. Most notably, our studies reveal that this Mr 28,000 fragment binds to neurofilaments, but the Mr 240,000 projection domain fails to interact. These data indicate that microtubules and neurofilaments share a common binding site on high-molecular-weight MAP-2.
我们开发了一种凝血酶蛋白水解切割方法,以获得更高产量的分子量为28,000的微管结合蛋白和分子量为240,000的微管投射蛋白,它们都是微管相关蛋白2(MAP-2)的组成部分。前者是一种高度碱性的成分,而后者以及完整的MAP-2都是酸性多肽。最值得注意的是,我们的研究表明,这个分子量为28,000的片段能与神经丝结合,但分子量为240,000的投射结构域却无法相互作用。这些数据表明,微管和神经丝在高分子量的MAP-2上共享一个共同的结合位点。