A 5' to 3' exonuclease functionally interacts with calf DNA polymerase epsilon.
收藏PubMed Central1992-10-15 更新2026-05-16 收录
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https://pmc.ncbi.nlm.nih.gov/articles/PMC50134/
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资源简介：
Analysis of fractions containing purified DNA polymerase epsilon from calf thymus has revealed the presence of a 5' to 3' exonuclease activity that is specific for a single strand of duplex DNA. This activity is capable of degrading a 3'-labeled oligonucleotide hybridized to M13mp18 DNA. When a second oligonucleotide primer is annealed 3 bases upstream, degradation of the downstream primer is strictly dependent on DNA synthesis from the upstream primer. Replacement of the downstream primer by an oligoribonucleotide of identical sequence results in a similar pattern of exonucleolytic activity. The activity has been highly purified and found to cosediment in glycerol gradients with a peptide of 56 kDa as judged by SDS/PAGE analysis. Effects of calf DNA polymerase alpha and delta on exonuclease activity are also observed but with differences in the pattern of products. IMAGES:
提供机构：
National Academy of Sciences
创建时间：
1992-10-15
