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Phosphorylation of terminal deoxynucleotidyl transferase in leukemic cells

Journal Article · · Biochem. Biophys. Res. Commun.; (United States)
 [1]; ; ;
  1. Univ. of New Mexico School of Medicine, Albuquerque
Phosphorylation of terminal deoxynucleotidyl transferase within leukemic cells has been demonstrated, using /sup 32/P labelling of intact cells in culture, followed by immunoprecipitation of the cellular extracts using an anti-terminal transferase antiserum. The phosphate linkage was found to involve serine and threonine residues. Purified calf thymus terminal transferase served as a substrate for cyclic AMP independent protein kinase obtained from leukemic cells. Phosphorylation in vitro of terminal transferase was accompanied by increased activity and decreased inhibition by excess ribo-ATP. These results indicate that terminal transferase is a physiologic cyclic AMP independent protein kinase substrate, and that this reaction may be important in its control.
OSTI ID:
6123887
Journal Information:
Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 106:2; ISSN BBRCA
Country of Publication:
United States
Language:
English