Purification and characterization of thymidine kinase from regenerating rat liver.
Biochim Biophys Acta
; 1079(3): 348-52, 1991 Sep 20.
Article
em En
| MEDLINE
| ID: mdl-1911861
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.
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Base de dados:
MEDLINE
Assunto principal:
Timidina Quinase
/
Fígado
/
Regeneração Hepática
Limite:
Animals
Idioma:
En
Ano de publicação:
1991
Tipo de documento:
Article