Human thymidine kinase: purification and some properties of the TK1 isoenzyme from placenta

Human thymidine kinase TK1 isoenzyme has been purified 1800-fold from placenta to a specific activity of 2.9 nmoles/min/mg of protein. The rapid purification procedure includes affinity chromatography on a thymidine-Sepharose column. At all stages of purification, the enzyme showed irreversible labi...

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Bibliographic Details
Published in:Molecular and cellular biochemistry 1982-11, Vol.45 (2), p.113-116
Main Authors: Ellims, P H, Gan, T E, Cosgrove, L
Format: Article
Language:English
Subjects:
Female
Humans
Isoenzymes - isolation & purification
Isoenzymes - metabolism
Kinetics
man
Nucleosides - pharmacology
placenta
Placenta - enzymology
Pregnancy
purification
Substrate Specificity
thymidine kinase
Thymidine Kinase - isolation & purification
Thymidine Kinase - metabolism
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Summary:Human thymidine kinase TK1 isoenzyme has been purified 1800-fold from placenta to a specific activity of 2.9 nmoles/min/mg of protein. The rapid purification procedure includes affinity chromatography on a thymidine-Sepharose column. At all stages of purification, the enzyme showed irreversible lability. The native molecular weight was determined to be 45000. Human placental TK1 exhibited specificity for ATP and thymidine as substrates, and significant inhibition was found only with thymidine nucleotides. TTP was the most effective inhibitor.
ISSN:0300-8177
1573-4919
DOI:10.1007/BF00223505