Lindahl T, Gally J A, Edelman G M
Proc Natl Acad Sci U S A. 1969 Feb;62(2):597-603. doi: 10.1073/pnas.62.2.597.
An exonuclease which specifically degrades double-standard DNA has been isolated from rabbit tissues. The enzyme has an approximate molecular weight of 42,000, requires a divalent metal ion as cofactor, and attacks DNA at the 5'-terminal ends, thereby liberating 5'-mononucleotides. It degrades several synthetic polydeoxynucleotides of single repeating base sequences more rapidly than DNA from natural sources. The specificity of this mammalian enzyme resembles that of several microbial enzymes (phage lambda exonuclease and DNA polymerase) which appear to be required for repair and recombination of DNA.
已从兔组织中分离出一种能特异性降解双链DNA的核酸外切酶。该酶的分子量约为42,000,需要二价金属离子作为辅因子,并从5'-末端攻击DNA,从而释放出5'-单核苷酸。与天然来源的DNA相比,它能更快地降解几种单一重复碱基序列的合成多脱氧核苷酸。这种哺乳动物酶的特异性类似于几种微生物酶(噬菌体λ核酸外切酶和DNA聚合酶),这些酶似乎是DNA修复和重组所必需的。