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1. The thymidine kinase from the African clawed frog Xenopus laevis has been purified by DEAE-cellulose chromatography and has a molecular weight of about 40 000. 2. Thymidine kinase is inhibited by low concentrations of ADP (Ki = 5 X 10(-7) M) and by thymidine (Ki = 3 X 10(-7) M) but not by GDP. 3. The pH optimum of the enzyme is 7.4. The enzyme is activated by low concentrations of dithiothreitol and markedly inhibited by SDS. 4. The pH-rate profile showed two ionizable groups with pK’ values of 7.8 and 9.2 and a pK’H value of 4.4. 5. The enzyme is activated by fluoride ions (K0.5 = 2 X 10(-3) M) and inhibited by hydroxylamine (Ki = 0.6 X 10(-5) M). 6. The Michaelis constant for thymidine is 1.1 X 10(-6) M. The values for ADP and ATP are 1 X 10(-5) M and 2.3 X 10(-5) M respectively. 7. The enzyme is activated by 20–60 mM Mg2+ and 5–30 mM Ca2+. 8. The enzyme is inhibited by 10–15 mM Zn2+ and 2–10 mM Cd2+. 9. No phosphorylation of either thymidine or dTMP was detected in the presence of the reduced form of the enzyme. 10. The inhibition constants for AMP and 2-amino-6-mercapto-1,3,4-triazine (ATP-alizarin complex) were determined and the results are consistent with the idea that the enzyme may be a two-subunit enzyme.”Bravo, you no longer exist”: the experience of job loss in an age of reduced working hours.
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