Purification and Characterization of Multiple Forms of Terminal Transferase from Human Leukemic Cells
Terminal deoxynucleotidyl transferase catalyzes the polymerization of deoxynucleoside triphosphates onto the 3’-OH terminus of a single stranded oligo(≥3 residues) or polydeoxynucleotide initiator. This non-template directed DNA polymerase was first detected in calf thymus tissue. Terminal transferase carries out, in the presence of divalent cation (Mg+2), a linear condensation polymerization reaction which is dependent solely on the concentration of 3’-OH groups and deoxynucleotide monomer. As a biochemical reagent, terminal transferase has enjoyed widespread popularity in the synthesis of defined oligomers and polymers, in recombinant DNA technology and in sequence analysis of oligodeoxynucleotides (reviewed by Bollum, 1981).1 The enzyme was purified to apparent homogeneity from calf thymus tissue by Chang and Bollum2 and was found to have an average native molecular weight of 32,000 and subunit molecular weights in SDS of 24,000 (β) and 8000 (α).
KeywordsAcute Lymphoblastic Leukemia Chronic Myelogenous Leukemia Blast Crisis Terminal Transferase Human Thymus
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