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  Volume: 21  Issue: 1  Pages: 44-48
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:
Citation:

Siluianova, S. N. (1975). Purification and some properties of the thymidine kinase from the rat thymus. Voprosy meditsinskoi khimii, 21(1), 44-48.
References
 1984 (vol 30)
 1983 (vol 29)
 1982 (vol 28)
 1981 (vol 27)
 1980 (vol 26)
 1979 (vol 25)
 1978 (vol 24)
 1977 (vol 23)
 1976 (vol 22)
 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)
 1965 (vol 11)