ABSTRACT. Two types of DNAligase, I and II, have been purified approximately 4,000-fold from mouse testes and 500-fold from nuclei of mouse spermatocytes. DNAligase I and II consisted of single polypeptides with molecular weights of 95,000 and 65,000, respectively, according to the estimation by SDS-polyacrylamide gel electrophoresis and the AMP-bindingassay. Ligase activities were higher in premeiotic spermatogonia and spermatocytes than those in liver and bone marrow cells. Moreover, DNAligase II showed rapid increase during meiotic prophase and a decrease in round spermatids. Since this behavior of DNAligase II is consistent with that of m-rec and DNApolymerase fi, both of which have been shown to be involved in DNArecombination in meiotic cells, DNAligase II might be an enzyme which works at the final step of meiotic recombination reaction.