RT Journal Article SR Electronic(1) A1 FOSTER, T. J. A1 HOWE, T. G. B.YR 1972 T1 Chloramphenicol Acetyl Transferase Formed by Wild-type and Complementing R Factors in Escherichia coli K12 JF Microbiology, VO 71 IS 3 SP 575 OP 580 DO https://doi.org/10.1099/00221287-71-3-575 PB Microbiology Society, SN 1465-2080, AB 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., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-71-3-575