[DNAses of the cell nuclei: Mn2+-dependent endonuclease].
Comparison of catalytic properties of a Mn2(+)-dependent and a Ca2+, Mg2+ dependent endonucleases of rat liver cell nuclei was carried out. The Mn2(+)-dependent endonuclease has Mr 31 kDa by SDS-PAAG-electrophoresis; pH optimum 5.5; calcium-magnesium synergism less than 3 in rat liver DNA, RF M13 DNA and phage M13 DNA. The rate of hydrolysis of single strand and double strand circular DNA was the same. The Mn2(+)-dependent endonuclease split DNA by double hit manner, and didn't change the manner in the presence of different divalent cations. Ca2+, Mg2(+)-dependent endonuclease has pH optimum 6.5; calcium-magnesium synergism up to 40 in rat liver DNA and 175 in RF M13 DNA. The rate of hydrolysis of single strand DNA was higher than double-strand DNA.
Bubnov
N V
NV
Basnak'ian
A G
AG
Botrin
I I
II
D000818:Animals; D002118:Calcium; D002384:Catalysis; D002467:Cell Nucleus / Q000201:enzymology*; D004247:DNA / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000378:metabolism; D003851:Deoxyribonucleases / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004720:Endonucleases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology; D008274:Magnesium; D008345:Manganese; D051381:Rats
D004277:DNA, Single-Stranded; D008345:Manganese; D004247:DNA; D003851:Deoxyribonucleases; D004720:Endonucleases; D008274:Magnesium; D002118:Calcium
DNKazy kletochnykh iader: Mn2+-zavisimaia éndonukleaza.