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Updated: Sep 13, 2026

In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 27, 2011
Site-specific endonuclease SscL1 I from strain Staphylococcus species L1
L Y Vasiljeva1, L A Zheleznaya, N I Matvienko
1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia. protres@sovam.com
Abstract:
A site-specific endonuclease SscL1 I preparation has been isolated and purified to near homogeneity from the strain Staphylococcus sp. L1 without admixtures of other nuclease activity. DNA cleavage proceeds according to the scheme: 5'-G down arrow ANTC-3' 3'-CTNA up arrow G-5', and thus the isolated enzyme is an isoschizomer of restriction endonuclease HinfI and belongs to the second class of restriction endonucleases. SscL1 I works over a broad range of temperature and pH. The enzyme is characterized by high stability during storage.

