Purification of cofilin, a 21,000 molecular weight actin-binding protein, from porcine kidney and identification of the cofilin-binding site in the actin sequence.

摘要: Cofilin, a 21,000 molecular weight protein originally purified from porcine brain that is capable of binding to actin filaments in molar ratio the monomer 1:1 filament (Nishida et al. (1984) Biochemistry 23, 5307-5313), was kidney present study. The two cofilins and were indistinguishable each other with respect mobility on polyacrylamide gel electrophoresis presence sodium dodecyl sulfate, one-dimensional peptide map, mode interaction actin. Treatment actin-cofilin complex zero-length cross-linker, 1-ethyl-3-[3-dimethylamino)propyl]carbodiimide (EDC), generated cross-linked product an apparent 63,000. Analysis this by mapping (Sutoh (1982) 21, 3654-3661) showed cofilin N-terminal segment containing residues 1-12.