R Factor-Controlled Restriction and Modification of Deoxyribonucleic Acid: Restriction Mutants

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Genetics of host-controlled restriction and modification of deoxyribonucleic acid in Escherichia coli.

Lederberg, Seymour (Brown University, Providence, R.I.). Genetics of host-controlled restriction and modification of deoxyribonucleic acid in Escherichia coli. J. Bacteriol. 91:1029-1036. 1966.-The locus for the host specific restriction and modification of deoxyribonucleic acid in Escherichia coli has been mapped by matings between mutants for these characters in strains K-12, C600, and B. Lin...

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Scale Efficiency in DEA and DEA-R with Weight Restriction

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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 Bacteriology

سال: 1972

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.112.3.1275-1279.1972