[Isolation and purification of nonspecific nuclease of cyanobacterium Plectonema boryanum CALU 465].
Nonspecific nuclease has been isolated from the cells of cyanobacterium Plectonema boryanum and purified to homogenic state. It has been established that the method of centrifugation of cell-free culture extract in the sucrose density gradient is efficient for the separation of pigment proteins and enzyme concentration. Under the successive use of two ion-exchangers the nuclease activity was determined in the concentration range of NaCl 0.065-0.085 M after separation of the cell-free cyanobacterium extract on the column with phosphocellulose in the range of 0.2-0.25 M, on the column with DEAE--Toyopearl respectively. The molecular mass of nuclease which is 40 kDa, has been determined by electrophoresis in polyacrylamide gel under denaturating conditions and gel-filtration on Sephadex G-100. It has been also established that the given enzyme is monosubunitary as to its structure.
Tsymbal
N V
NV
Institute of Microbiology and Virology, National Academy of Sciences of Ukraine, Kyiv.
Samoĭlenko
V A
VA
Syrchin
S A
SA
Mendzhul
M I
MI
D002482:Cellulose / Q000031:analogs & derivatives*; D002498:Centrifugation; D000458:Cyanobacteria / Q000201:enzymology*; D003851:Deoxyribonucleases / Q000737:chemistry / Q000302:isolation & purification*; D004983:Ethanolamines; D007474:Ion Exchange; D008970:Molecular Weight; D013395:Sucrose
D004983:Ethanolamines; D013395:Sucrose; D002482:Cellulose; C008881:phosphocellulose; D003851:Deoxyribonucleases; C007369:2-diethylaminoethanol