Abstract

An enzymatic activity, having the properties expected of a B-specific host-controlled modification enzyme, has been purified from an extract of Escherichia coli strain B. This activity renders the unmodified replicative form of phage fd resistant to B-specific restriction and is only present in strains carrying intact genes for type B modification. In phosphate buffer, the enzyme acts optimally at pH 6 and is dependent upon a single cofactor, S-adenosylmethionine.

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