Open AccessDeoxyribonucleotide Phosphatase from Rat Liver and Cultured Mouse Fibroblasts
Author(s) -
Magnusson Göran
Publication year - 1971
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1971.tb01384.x
Subject(s) - dephosphorylation , deoxyribonucleotide , enzyme , biochemistry , phosphatase , microbiology and biotechnology , deoxyribonucleotides , chemistry , deoxyguanosine , phosphate , deoxyuridine , thymidine , enzyme assay , biology , dna , nucleotide , gene , oligonucleotide
An enzyme which catalyzes the preferential dephosphorylation of the 5′‐phosphates of deoxythymidine, deoxyuridine and deoxyguanosine was purified 100‐fold from rat liver. The preparation appeared to be free from contaminating phosphatase activities. The dephosphorylation of deoxyribonucleotides was dependent on the presence of Mg 2+ ions and had a pH optimum around 6.0. The K m value for the dephosphorylation of deoxythymidine 5′‐phosphate was 5.7 mM. High activities of the enzyme were found in cultured mouse fibroblasts. In parasynchronously growing cells no changes of enzyme activity were found during the cell cycle.