O'Reilly G, Clarke F
Faculty of Science and Technology, Griffith University, Nathan, Australia.
FEBS Lett. 1993 Apr 19;321(1):69-72. doi: 10.1016/0014-5793(93)80623-3.
Fragmentation of the actin binding glycolytic enzyme, aldolase, with cyanogen bromide yields an 18K actin binding fragment which corresponds to residues 1-164 of the aldolase sequence. Within this fragment there is a region of sequence (residues 32-52) which is highly homologous to a region of sequence near the C-terminus of actin itself and which is also found in the actin binding domains of a number of other actin binding proteins. A synthetic peptide corresponding to the aldolase sequence 32-52 encompassing this region of homology binds to F-actin and specifically competes with native aldolase for binding to this cytoskeletal protein.
用溴化氰裂解肌动蛋白结合糖酵解酶醛缩酶,可产生一个18K的肌动蛋白结合片段,该片段对应于醛缩酶序列的第1至164位残基。在这个片段内,有一个序列区域(第32至52位残基),它与肌动蛋白自身C末端附近的一个序列区域高度同源,并且在许多其他肌动蛋白结合蛋白的肌动蛋白结合结构域中也能找到。一个对应于醛缩酶序列32 - 52位、包含该同源区域的合成肽可与F - 肌动蛋白结合,并特异性地与天然醛缩酶竞争结合这种细胞骨架蛋白。