Abstract
Rabbit skeletal muscle actin labeled with 125I by an enzymic method is capable of polymerization and to bind to matix-bound pancreatic DNAse I like unlabeled G-actin. Actin can be released from DNAse-I-agarose by 35-40% formamide. Actin which was only shortly exposed to this solvent was able to bind again to DNAse I and to form filaments indicating that it was recovered functionally intact from the affinity matrix.