PMID: 1911861Sep 20, 1991

Purification and characterization of thymidine kinase from regenerating rat liver

Biochimica Et Biophysica Acta
I TsukamotoS Kojo

Abstract

Thymidine kinase (EC 2.7.1.21) 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.

References

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Dec 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·A J Murphy, A Efstratiadis
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Nov 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·P F LinF H Ruddle
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Sep 2, 2011·Chemistry : a European Journal·Henri A van KalkerenFloris L van Delft

Related Concepts

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

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