Abstract
CYP2E1 is the main enzyme responsible for chlorzoxazone 6-hydroxylase activity in human liver. Here, it is shown that marmoset monkey liver microsomal fraction catalyses this reaction at a similar rate and with a similar Km to human liver and that the activity is increased 4-fold in marmosets treated with isoniazid, a known inducer of CYP2E1. This indicates that CYP2E1 is present in marmoset liver. However conversely, an anti-peptide antibody targeted against the C-terminus of human and cynomolgus monkey CYP2E1 (Val-Ile-Pro-Arg-Ser) failed to bind to marmoset monkey hepatic microsomal fraction. To investigate if there is a difference in the C-terminus of CYP2E1 in these species, this region of marmoset CYP2E1 was sequenced following amplification of marmoset liver cDNA with primers selected according to conserved regions identified in human and cynomolgus monkey CYP2E1. It was found that the deduced amino acid sequence of marmoset CYP2E1 in this region is very similar to human CYP2E1, but due to two base differences in the marmoset nucleic acid sequence, the C-terminus of marmoset CYP2E1 is extended by 2 amino acids, i.e. Val-Ile-Pro-Arg-Ser-Ser-Val. This difference is sufficient to prevent the binding of an antibody raised aga...Continue Reading
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