An ADPase from sarcoplasmic reticulum of rabbit muscle cleaves ADP bound to F-actin.

We have found that sarcoplasmic reticulum from rabbit muscle contains an ADPase which cleaves ADP bound to F-actin. The interaction is not of the simple Michaelis-Menten type, the order of the reaction being larger than the first. A possible explanation of this behaviour could be that ADPase binds to two adjacent actin monomers with a preferred orientation thus cleaving preferentially the nucleotide of one of the two monomers.