A site-specific endonuclease SscL1 I preparation has been isolated and
purified to near homogeneity from the strain Staphylococcus sp. L1 wi
thout admixtures of other nuclease activity. DNA cleavage proceeds acc
ording to the scheme: 5'-G down arrow ANT C-3' 3'-C TNA up arrow G-5',
and thus the isolated enzyme is an isoschizomer of restriction endonu
clease HinfI and belongs to the second class of restriction endonuclea
ses. SscL1 I works over a broad range of temperature and pH. The enzym
e is characterized by high stability during storage.