Mammalian liver contains an activity which mimics bacterial chloramphenicol acetyltransferase.
Rat liver extracts contain an activity which mimics Escherichia coli chloramphenicol acetyltransferase (CAT); the latter is commonly used to report transcriptional activation of chimeric genes transfected into cultured cells. Although the activities are indistinguishable by the standard thin-layer chromatography assay, alternate methods can discriminate between them. The rat CAT-like activity appears to be an integral membrane protein. It was observed in the microsomal fraction of both liver and kidney. Similarly CAT-like activities were detected in mouse, rabbit and pig liver. In addition, liver homogenates which contain the CAT-like activity also contain a heat-labile inhibitor of (authentic) bacterial CAT.
De Maio
A
A
Department of Surgery, Johns Hopkins University School of Medicine, Baltimore, MD.
Buchman
T G
TG
D000818:Animals; D002460:Cell Line; D015500:Chloramphenicol O-Acetyltransferase / Q000378:metabolism*; D002855:Chromatography, Thin Layer / Q000379:methods; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000201:enzymology; D008099:Liver / Q000201:enzymology*; D008115:Liver Regeneration; D008565:Membrane Proteins / Q000378:metabolism; D051381:Rats; D013045:Species Specificity; D013347:Subcellular Fractions / Q000201:enzymology; D014018:Tissue Distribution
D008565:Membrane Proteins; D015500:Chloramphenicol O-Acetyltransferase