[Isolation of Ca2+, Mg2+-dependent nuclease from calf thymus chromatin].
Ca2+,Mg2+-dependent nuclease was isolated from calf thymus chromatin by stepwise chromatography on DEAE-Sepharose, CM-Sephadex and DNA-Sepharose. The enzyme was purified more than 700-fold. SDS-PAGE electrophoresis revealed one protein band possessing an enzymatic activity. The molecular mass of the nuclease as determined by gel filtration is 25700 Da, that determined by 12% SDS polyacrylamide gel electrophoresis is 28,000 Da. In the presence of various ions the enzyme activity decreases in the following order: (Ca2+ + Mn2+) greater than (Ca2+ + Mg2+) greater than Mn2+; the pH optimum is at 8.0. In media with Mg2+, Ca2+, Co2+ and Zn2+ the nuclease is inactive. Some other properties of the enzyme are described.
Nikonova
L V
LV
Zotova
R N
RN
Umanskiĭ
S R
SR
D000818:Animals; D002417:Cattle; D002843:Chromatin / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004706:Endodeoxyribonucleases / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D013950:Thymus Gland / Q000201:enzymology*
D002843:Chromatin; D004706:Endodeoxyribonucleases; C029367:calcium magnesium dependent endodeoxyribonuclease
Vydelenie Ca2+, Mg2+-zavisimoĭ nukleazy iz khromatina timusa telenka.