PMID: 1911861Sep 20, 1991

Purification and characterization of thymidine kinase from regenerating rat liver

Biochimica Et Biophysica Acta
I TsukamotoS Kojo


Thymidine kinase (EC from regenerating rat liver has been purified 70,000-fold to apparent homogeneity by affinity chromatography. Molecular weight of the native enzyme was found to be about 54,000, as determined by gel filtration. Electrophoresis in polyacrylamide gels containing sodium dodecyl sulfate yielded a single band with a molecular weight of 26,000, suggesting that thymidine kinase is a dimer of very similar or identical subunits. The Michaelis constant for thymidine is 2.2 microM. ATP acts as a sigmoidal substrate with a 'Km' of 0.2 mM. Reaction kinetics and product inhibition studies reveal the enzymatic mechanism to be sequential.


Jan 1, 1976·Preparative Biochemistry·E P Kowal, G Markus
Jan 1, 1976·Analytical Biochemistry·A Bensadoun, D Weinstein
Dec 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·A J Murphy, A Efstratiadis
Mar 1, 1986·Biochemical Pharmacology·R NakataS Kojo
Sep 1, 1987·Biochemical Pharmacology·I Tsukamoto, S Kojo
Feb 15, 1985·Biochemical Pharmacology·R NakataS Kojo
Nov 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·P F LinF H Ruddle
Jan 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·Y F Lau, Y W Kan
Sep 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·H D Bradshaw
Feb 28, 1983·Biochemical and Biophysical Research Communications·M H Lai, G Weber
Sep 2, 2011·Chemistry : a European Journal·Henri A van KalkerenFloris L van Delft

Related Concepts

Magnesium ADP
Chromatography, Affinity
Molecular Sieve Chromatography
Liver Regeneration
August Rats
Substrate Specificity
Thymidine Kinase

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