[Isolation and physico-chemical properties of homogenous nuclease from Serratia marcescens].
A simplified procedure for purification of nuclease from Serratia marcescens, including chromatography on DEAE- and phosphocellulose in a stationary regime has been developed. The method described results in a physically homogenous enzyme, which does not contain phosphatase, phosphodiesterase or proteinase admixtures. The molecular weight of the enzyme as determined by polyacrylamide gel electrophoresis is 33 000 +/- 10%. p-Chloromercurybenzoate (10(-2) M) completely inactivates the enzyme, while beta-mercaptoethanol (0,64 M) in the presence of 2 M urea causes only partial inactivation of the enzyme. Urea (4 or 7 M), when added to the reaction mixture, increases the enzyme activity 2,2-, 1,7- and 1,4-fold as compared to native, denaturated DNA and RNA, respectively.
D004706:Endodeoxyribonucleases; D004720:Endonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004722:Endoribonucleases; D007700:Kinetics; D008970:Molecular Weight; D012706:Serratia marcescens / Q000201:enzymology*
D004706:Endodeoxyribonucleases; D004720:Endonucleases; D004722:Endoribonucleases; C021835:Serratia marcescens nuclease
Poluchenie nukleazy Serratia marcescens v gomogennom sostoianii i izuchenie fiziko-khimicheskikh svoistv fermenta.