[Isolation and some properties of Ca2+-, Mg2+-dependent deoxyribonuclease from sea urchin (Strongylocentrotus intermedius) embryos].
Ca2+-Mg2+-dependent deoxyribonuclease (deoxyribonucleate-5'-oligonucleotidehydrolase E. C. 3.1.4.5). Molecular weight of the enzyme is found to be 40 000 daltons isoelectric point--4.4. The enzyme degraded DNA only in the presence of bivalent cations. It hydrolyses preferentially native DNA with pH optimum 7.0-7.2 in the presence of Mg2+ ions. Ca2+ ions shift the pH optimum to 8.0-8.5. Combined addition of Ca2+ and Mg2+ ions results in a sinergic effect and changes the enzyme specificity to the secondary DNA structure. The enzyme hydrolyses both native and denatured DNA by the endonucleolytic type to form oligonucleotides with 5' terminal phosphate the content of tetra-octanucleotides being 80-85%.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D003851:Deoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism*; D004625:Embryo, Nonmammalian / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008274:Magnesium / Q000494:pharmacology; D008970:Molecular Weight; D009691:Nucleic Acid Denaturation; D012617:Sea Urchins; D013329:Structure-Activity Relationship
D003851:Deoxyribonucleases; D008274:Magnesium; D002118:Calcium
Vydelenie i nekotorye svoĭstva Ca2+, Mg2+-zavisimoĭ dezoksiribonykleazy iz embrionov morskogo ezha Strongylocentrotus intermedius