Deoxyribonuclease II from porcine spleen has a molecular weight of 38 kDa. The enzyme is a glycoprotein endonuclease with dimeric structure. Optimum pH range is 4.5-5.0 at ionic strength 0.15 M. Deoxyribonuclease II (Acid DNase) hydrolyzes deoxyribonucleotide linkages in native and denatured DNA yielding products with 3'-phosphates. It also acts on p-nitrophenylphosphodiesters at pH 5.6-5.9. Bernardi (BBRC, 17, 573, 1971) describes a three stage degradation of native DNA by DNase II. DNase II has been used to treat transformed cells during the purification of β-lactamase. It has also been used for the preparation of adenoma tissue in a study that investigated the effect of somatoprim on growth hormone secretion in human adenoma cell cultures (hSA). Deoxyribonuclease II from bovine spleen has been used in a study that conducted a partial purification of deoxyribonucleases from eggs and liver of Xenopus laevis. Deoxyribonuclease II from bovine spleen has also been used in a study to investigate nucleic acid and protein synthesis of splenic lymphocytes.