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- W2065400558 abstract "Methods of extraction and assay of terminal deoxynucleotidyl transferase (TdT) from human lymphoblasts and calf thymus were compared. A high salt concentration was mandatory for complete enzyme extraction, while dialysis of the crude extract resulted in a major loss of enzyme activity. In addition, TdT was partially purified from lymphoblasts of patients with acute lymphoblastic leukemia. The Km for the monomer, deoxy-guanosine 5′-triphosphate (dGTP), is high (~0.1 mm) in the presence of either Mg2+ or Mn2+, whereas the Km for the initiator, poly(deoxyadenylic acid [poly(d(pA)50)], with an average chain length of 50 residues, is 2.5 μm in the presence of Mg2+ and 0.3 μm in the presence of Mn2+. The maximum velocity is higher for the calf thymus TdT in the presence of Mg2+ than in Mn2+. Human TdT catalyzes the polymerization of dGTP at a higher rate in the presence of Mn2+ than with Mg2+. These data illustrate that partially purified human TdT differs in catalytic properties from the purified calf thymus enzyme. Therefore, optimal conditions for assay of TdT in extracts from calf and human tissues differ." @default.
- W2065400558 created "2016-06-24" @default.
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- W2065400558 date "1977-08-01" @default.
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- W2065400558 title "Terminal deoxynucleotidyl transferase: Characterization of extraction and assay conditions from human and calf tissue" @default.
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- W2065400558 doi "https://doi.org/10.1016/0003-9861(77)90533-1" @default.
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