Open AccessAn Endonuclease from Mouse Cells Specific for Single‐Stranded DNA
Author(s) -
OTTO Bernd,
KNIPPERS Rolf
Publication year - 1976
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1976.tb11153.x
Subject(s) - endonuclease , dna , dna supercoil , chemistry , oligonucleotide , enzyme , microbiology and biotechnology , covalent bond , biochemistry , restriction enzyme , biophysics , biology , dna replication , organic chemistry
An endonuclease with a molecular weight of about 70000 (5–6 S) was extensively purified from mouse ascites cells. The enzyme specifically attacks single‐stranded DNA which is degraded mainly to oligonucleotides, with 5–10 residues. Supercoiled covalently closed circular phage DNA is converted to the linear relaxed form. The enzyme activity is highly sensitive to salt and can be stimulated by reagents lowering the dielectric constant of the buffer such as dimethylsulfoxide and glycerol.