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. 1982 Apr 1;203(1):77-84.
doi: 10.1042/bj2030077.

The SalGI restriction endonuclease. Purification and properties

A Maxwell, S E Halford

The SalGI restriction endonuclease. Purification and properties

A Maxwell et al. Biochem J. .

Abstract

The type II restriction endonuclease SalGI has been purified to near homogeneity. At least 80% of the protein remaining after the final stage of the preparation is SalGI restriction endonuclease; no contaminating nucleases remain detectable. The principal form of the protein under both native and denaturing conditions is a monomer of M(r) about 29000. The optimal conditions for both enzyme stability and enzyme activity have been determined.

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