Chloramphenicol Acetyl Transferase Formed by Wild-type and Complementing R Factors in Escherichia coli K12 Free

Abstract

Summary

Chloramphenicol acetyl transferase (CAT) was purified from K12 carrying R1 and 222 and from K12 (R1 Cm /R100-99 TcCm). The third enzyme has a lower affinity for chloramphenicol and greater heat lability than those specified by R1 and 222, compatible with the enzyme's resulting from interallelic complementation. CAT has a molecular weight of 80000, with subunits of 20000. Material cross reacting with anti-222 CAT serum was detected in Cm mutant cell sonicates.

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/content/journal/micro/10.1099/00221287-71-3-575
1972-08-01
2024-03-29
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