The SalGI restriction endonuclease. Purification and properties
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چکیده
منابع مشابه
Restriction endonuclease RsrI from Rhodobacter sphaeroides, an isoschizomer of EcoRI: purification and properties.
We have purified RsrI endonuclease (R.RsrI), an isoschizomer of EcoRI, from Rhodobacter sphaeroides strain 630. The enzyme is homogeneous as judged by polyacrylamide gel electrophoresis and size-exclusion high-performance liquid chromatography. RsrI endonuclease is a dimer over the concentration range of 0.05 to 1.4 mg/ml. The reduced and denatured molecular weight of the enzyme is 30,000 Da. R...
متن کاملCatalytic and DNA binding properties of PvuII restriction endonuclease mutants.
The role of particular residues of the PvuII endonuclease in DNA binding and cleavage was studied by mutational analysis using a number of in vivo and in vitro approaches. While confirming the importance of residues predicted to be involved directly in function by the crystal structure, the analysis led to several striking results. Aspartate 34, which contacts the central base pair of the PvuII...
متن کاملThe Deoxyribonucleic Acid Modification and Restriction Enzymes of Escherichia coli B II. PURIFICATION, SUBUNIT STRUCTURE, AND CATALYTIC PROPERTIES OF THE RESTRICTION ENDONUCLEASE*
The restriction endonuclease of Escherichia coli B has been purified and is free of nonspecific endonuclease. On sucrose gradients it sediments in a broad band with an sqO,W of 11 through 18. As judged by polyacrylamide gel electrophoresis the enzyme exists in at least two active forms, each of which possess three nonidentical polypeptides, (Y, /3, and y, of molecular weights 135,000,60,000, an...
متن کاملThe deoxyribonucleic acid modification and restriction enzymes of Escherichia coli B. II. Purification, subunit structure, and catalytic properties of the restriction endonuclease.
The restriction endonuclease of Escherichia coli B has been purified and is free of nonspecific endonuclease. On sucrose gradients it sediments in a broad band with an sqO,W of 11 through 18. As judged by polyacrylamide gel electrophoresis the enzyme exists in at least two active forms, each of which possess three nonidentical polypeptides, (Y, /3, and y, of molecular weights 135,000,60,000, an...
متن کاملThe Deoxyribonucleic Acid Modification and Restriction Enzymes of Escherichia coli B II. PURIFICATION, SUBUNIT STRUCTURE, AND CATALYTIC PROPERTIES OF THE RESTRICTION ENDONUCLEASE*
The restriction endonuclease of Escherichia coli B has been purified and is free of nonspecific endonuclease. On sucrose gradients it sediments in a broad band with an sqO,W of 11 through 18. As judged by polyacrylamide gel electrophoresis the enzyme exists in at least two active forms, each of which possess three nonidentical polypeptides, (Y, /3, and y, of molecular weights 135,000,60,000, an...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1982
ISSN: 0264-6021
DOI: 10.1042/bj2030077