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Structure of Calf Thymus Terminal Deoxynucleotidyl Transferase

  • Lucy M. S. Chang
  • F. J. Bollum
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 145)

Abstract

Terminal deoxynucleotidyl transferase (TdT), originally purified from calf thymus glands to homogeneity, was shown to have a native molecular weight of 32,000 by equilibrium sedimentation and two peptides of 26,500-dalton and 8,000-dalton when analyzed by gel electrophoresis in the presence of sodium dodecyl sulfate (SDS) (1). Rabbit antibody prepared against this homogeneous TdT preparation (2) precipitates a single 58,000-dalton peptide from cell extracts of human and mouse leukemia lines labeled with radioactive amino acids (3). A high molecular weight enzyme (62,000-dalton peptide) was also purified from human leukemic lymphoblasts (4).

Keywords

Ammonium Sulfate Terminal Deoxynucleotidyl Transferase Ammonium Sulfate Fraction Sepharose Column Enzyme Fraction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Lucy M. S. Chang
    • 1
  • F. J. Bollum
    • 1
  1. 1.Uniformed Services University of the Health SciencesBethesdaUSA

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