Catalytic properties of the HhaII restriction endonuclease.

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The 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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The 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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The 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