Terminal deoxynucleotidyl transferase in rooster sperm

摘要: A 165,000g pellet fraction, isolated from lysed rooster spermatozoa, was shown to contain a deoxynucleotide polymerizing activity which banded in sucrose at buoyant density of 1.15gm/ml. The solubilized enzyme, partially purified by gel filtration, estimated have molecular weight 33,000 and utilized dT10 or dG10 as exogenous primers template-independent reactions sensitive either sodium pyrophosphate ethylenediaminetetra- cetic acid. Pyrimidine nucleotides (dTTP) were preferentially polymerized the presence Co++, while purine (dGTP) preferred substrate when Mn++ divalent cation. These properties are all consistent with those terminal deoxynucleotidyl transferase. An enzyme similar also obtained subjecting sperm lysate procedure isolate transferase calf thymus. It is hypothesized that may be involved regulation gene expression during embryogenesis.