[Isolation and properties of endodeoxyribonuclease from the ovicells of the loach].
A new DNAase was isolated from unfertilized loach eggs. The enzyme is activated by bivalent metal ions (Mg2+, Ca2+, Mn2+) and is inhibited by Na+ and N-ethylmaleimide. The maximal activity of DNAase lies within the pH range of 9.0-9.5. The enzyme is thermostable and predominantly hydrolyzes the two-chain DNA by producing one-chain ruptures. The DNAase activity during the purification procedure and enzymatic analysis was determined by a highly sensitive method based on registration of superhelical plasmid or phage DNA conversion into open circular or linear molecules.
D000818:Animals; D002413:Cations, Divalent; D004706:Endodeoxyribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D005260:Female; D005399:Fishes; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010063:Ovum / Q000201:enzymology*
D002413:Cations, Divalent; D004706:Endodeoxyribonucleases
Vydelenie i svoĭstva éndodezoksiribonukleazy iz iaĭtsekletok v'iuna.