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Updated: Aug 14, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP
Published on: May 26, 2017
The dual activity of pyruvate kinase type M2 from chromatin extracts of neoplastic cells
Jan Ignacak1, Maria Barbara Stachurska
1Department of General Biochemistry, Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, 7 Kopernika Street, 31-034 Cracow, Poland. mbignaca@cyf-kr.edu.pl
Abstract:
Pyruvate kinase type M(2) from Morris hepatoma 7777 tumour cell nuclei and cytosol, in contrast to types L and M(2) from nuclei and cytosol of normal rat liver, shows the histone H(1) kinase activity. Moreover, in the presence of L-cysteine and without ADP it converts 2-phosphoenolpyruvate (PEP) to pyruvate while in the presence of L-arginine or L-histidine does not. L-Cysteine markedly stimulates the activity of histone H(1) kinase transferring a phosphate group from PEP to, as results suggested, the epsilon -amino group of L-lysine of histone H(1). This, L-cysteine which is known to inhibit the activity of pyruvate kinase type M(2) from neoplastic cells transfering a phosphate from PEP to ADP, can act as a control factor champing the direction of enzymatic reaction in cancer cells.
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