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A screening procedure was used to isolate a number of mutants of Escherichia coli K-12 with low penicillinase activity. By co-transduction with purA, three of the mutants were found to map near 82 min. Penicillinase was purified from one mutant and from a transductant with a temperature-sensitive enzyme. Comparison with wild-type penicillinase revealed similarities in the Ouchterlony immunodiffusion test but differences in the catalytic properties. It is concluded that the mutations have occurred in the structural gene of the chromosomal penicillinase (designated ampC). Purified enzyme and a temperature-sensitive mutant were used to investigate whether the penicillinase has a physiological function related to biosynthesis or breakdown of murein. No positive evidence for any such function was obtained.
L G Burman, and
J T Park, and
E B Lindström, and
H G Boman
January 1970,
Journal of bacteriology,
L G Burman, and
J T Park, and
E B Lindström, and
H G Boman
October 1968,
Genetical research,
L G Burman, and
J T Park, and
E B Lindström, and
H G Boman
October 1977,
Journal of bacteriology,
L G Burman, and
J T Park, and
E B Lindström, and
H G Boman
January 1970,
Journal of bacteriology,
L G Burman, and
J T Park, and
E B Lindström, and
H G Boman
May 1966,
Journal of bacteriology,
L G Burman, and
J T Park, and
E B Lindström, and
H G Boman
October 1968,
Bollettino della Societa italiana di biologia sperimentale,
L G Burman, and
J T Park, and
E B Lindström, and
H G Boman
May 1964,
Journal of molecular biology,
L G Burman, and
J T Park, and
E B Lindström, and
H G Boman
July 1973,
Israel journal of medical sciences,
L G Burman, and
J T Park, and
E B Lindström, and
H G Boman
January 1967,
Pathologia et microbiologia,
L G Burman, and
J T Park, and
E B Lindström, and
H G Boman
April 1966,
Lancet (London, England),
