title: The major fraction of deoxyribonuclease activity from human urinary proteins. Purification and properties.
abstract: The major fraction of deoxyribonuclease activity from human urinary protein was purified 40-fold in about 14% yield. The enzyme shows an isoelectric point at pH 4.2 and has a molecular weight of 33,600+/-3,000. Optimum activity was shown at pH 6.8 in the presence of 12.5 mmol/l Mg2+ plus 1 mmol/l Ca2+. The enzymic reaction is inhibited by high ionic strength (greater than 300 mmol/l Na+). The purified enzyme readily hydrolyzes native DNA to oligodeoxyribonucleotides with an average chain length of 5.3+/-0.2 after exhaustive digestion. Therefore, this endonuclease may be designated as neutral deoxyribonuclease (deoxyribonucleate oligonucleotidohydrolase, EC 3.1.4.5).
mesh_terms: D003851:Deoxyribonucleases / Q000302:isolation & purification / Q000652:urine*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D011507:Proteinuria; D013056:Spectrophotometry, Ultraviolet
chemical_list: D003851:Deoxyribonucleases