{Reference Type}: Journal Article
{Title}: Further purification and characterization of human 3-methyladenine-DNA glycosylase. Evidence for broad specificity.
{Author}: Gallagher PE;Brent TP;
{Journal}: Biochim Biophys Acta
{Volume}: 782
{Issue}: 4
{Year}: Sep 1984 10
暂无{DOI}: 10.1016/0167-4781(84)90045-9
{Abstract}: Further purification of a human placental 3-methyladenine-DNA glycosylase by phosphocellulose column chromatography yielded a 6000-fold increase in specific activity with greater than 5% recovery. Although 3-methyladenine was the predominant base released from double-stranded methylated DNA by this enzyme, minor releasing activities for 7-methylguanine and 3-methylguanine were also observed. During purification, the three DNA glycosylase activities consistently copurified with constant ratios of specific activity. Moreover, all the activities were heat-inactivated at 50 degrees C at the same rate, required double-stranded methylated DNA as substrate, were inhibited by spermine and spermidine, and were not subject to product inhibition. These data strengthen the likelihood that the three activities are associated with a single DNA glycosylase.