Voprosy meditsinskoi khimii (ISSN 0042-8809)

Purification and some properties of the thymidine kinase from the rat thymus

   
Siluianova S.N.
PubMed Id: 1119111
Year: 1975 vol: 21  issue:1  pages: 44-48
Abstract: Preparation of thymidine kinase, purified 500-fold, was isolated from rat thymus by means of fractionation with ammonium sulphate, gel filtration on Sephadex G-200, treatment with calcium phosphate gel and chromatography on DEAE-cellulose. The enzyme was shown to be stabilized by 0.12 mM of thymidine, activated by Mg2 (optimum concentration 12 mM) and inhibited by Mn2+ATP served as donor of phosphate groups in reactions, catalyzed by thymidine kinase. In respect to the phosphate acceptor the enzyme showed sharp specificity: it used as a substrate only thymidine, deoxyuridine and its derivatives, substituted at the 5-th position by haloid group. In study of affinity of the enzyme for the substrate Km equals 2.5-10 minus 5 M (Vmax equals 0.09) was determined.
Download PDF:
Reference: Siluianova S.N., Purification and some properties of the thymidine kinase from the rat thymus, Voprosy meditsinskoi khimii, 1975, vol: 21(1), 44-48.
References
 1975(Vol:21)
 1974(Vol:20)
 1973(Vol:19)
 1972(Vol:18)
 1971(Vol:17)
 1970(Vol:16)
 1969(Vol:15)
 1968(Vol:14)
 1967(Vol:13)
 1966(Vol:12)