Catalytic properties of the HhaII restriction endonuclease.
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چکیده
منابع مشابه
Catalytic 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...
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15 صفحه اولThe 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: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)95742-x