title: The SalGI restriction endonuclease. Purification and properties.
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.
mesh_terms: D002413:Cations, Divalent / Q000494:pharmacology; D004247:DNA / Q000378:metabolism; D004262:DNA Restriction Enzymes / Q000302:isolation & purification* / Q000378:metabolism; D015252:Deoxyribonucleases, Type II Site-Specific; D004355:Drug Stability; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D013379:Substrate Specificity
chemical_list: D002413:Cations, Divalent; D004247:DNA; D004262:DNA Restriction Enzymes; D015252:Deoxyribonucleases, Type II Site-Specific; C029792:GTCGAC-specific type II deoxyribonucleases