Terminal deoxynucleotidyltransferase was isolated and partially purified from nuclei from white blood cells of a patient with chronic myelogenous leukemia. The terminal transferase has a sedimentation value of 3.4 S, a pH optimum of 7.5, a Mn2+ optimum of 0.1 mm, and a Mg2+ optimum of 5 to 7 mm. The purified enzyme efficiently utilizes a number of DNA primers but not RNA primers. The presence of this enzyme in human myelogenous leukemic cells suggests that its presence may be associated with a particular stage of the disease rather than being specific for a particular form of leukemia or for thymic cells.
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Sarin et al. (1974) studied this question.
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