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- W1546247896 abstract "Abstract We have purified an acid-soluble DNA endonuclease, termed nuclease gamma, from Ustilago cell extracts. The enzyme is nearly homogeneous, purified 1700-fold. The protein appears to be globular with a molecular weight in the range 17,000 to 21,000. It requires a divalent cation and is optimally active at slightly alkaline pH. The enzyme prefers duplex DNA as substrate but will slowly cleave single-stranded DNA. Cleavage of covalently closed duplex DNA is unaltered by changes in superhelix density. Divalent cations direct the mode by which the enzyme cleaves duplex DNA. When Mg2+ or Ca2+ is added, the enzyme nicks one strand of the duplex. When Mn2+, Co2+, or Zn2+ is added, the enzyme can introduce double strand breaks. Oligonucleotides terminated with 5'-phosphoryl and 3'-hydroxyl groups are the products of hydrolysis. DNA fragments generated can be religated to linear pBR322 DNA with completely base-paired ends." @default.
- W1546247896 created "2016-06-24" @default.
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- W1546247896 date "1984-03-01" @default.
- W1546247896 modified "2023-09-30" @default.
- W1546247896 title "Purification and properties of nuclease gamma from Ustilago maydis." @default.
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- W1546247896 doi "https://doi.org/10.1016/s0021-9258(17)43253-4" @default.
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