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

1972; Microbiology Society; Volume: 71; Issue: 3 Linguagem: Inglês

10.1099/00221287-71-3-575

2059-9323

T. J. Foster, T. G. B. Howe,

DNA Repair Mechanisms

Summary Chloramphenicol acetyl transferase (CAT) was purified from Escherichia coli K12 carrying R1 and 222 and from E. coli K12 recA (R1 Cm8 7/R100-99 TcRCmS). 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 CmS mutant cell sonicates.