[Various properties of immobilized terminal deoxynucleotidyl transferase from the cattle thymus].
The effects of temperature, pH, and concentration of sodium cacodylate buffer on the activity of partially purified terminal deoxynucleotidyl transferase from cattle thymus immobilized on BrCN-Sepharose were studied. The enzyme retained at least 60% of the initial activity after 6 h of incubation at 30 degrees in 50 mM potassium phosphate buffer, pH 7.2 in the absence of substrate. Short-term activation of the enzyme during incubation was noticed. The maximum activity of the immobilized preparations was observed in 240-280 mM sodium cacodylate buffer in the reaction mixture, pH 7.5-7.9 at 37-40 degrees.
Akishev
A G
AG
D000818:Animals; D002417:Cattle; D004253:DNA Nucleotidylexotransferase / Q000032:analysis*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D013696:Temperature; D013950:Thymus Gland / Q000201:enzymology*; D013997:Time Factors
D004800:Enzymes, Immobilized; D004253:DNA Nucleotidylexotransferase
Izuchenie nekotorykh svoĭstv immobilizovannoĭ terminal'noĭ dezoksinukleotidiltransferazy iz timusa krupnogo rogatogo ckota.