抄録
DNase I affinity chromatography has been known to be a useful tool for analysis of G-actin binding proteins in various kinds of nonmuscle cells. Here we coupled DNase I to an agarose gel in the presence of PMSF, as DNase I fractions purified from bovine pancrease contain serine-threonine type protease activities. By the use of the DNase I affinity column obtained, a 68 kD component was purified from the soluble cytoplasmic protein fraction of bovine liver and identified as a membrane-to-actin cytoskeleton linker, annexin VI.
