Qs. Jiang et al., MOLECULAR-CLONING AND SEQUENCING OF A GUINEA-PIG CYTOCHROME P4502D (CYP2D16) - HIGH-LEVEL EXPRESSION IN ADRENAL MICROSOMES, Biochemical and biophysical research communications, 209(3), 1995, pp. 1149-1156
Studies were done to characterize a guinea pig adrenal microsomal P450
that had been linked with xenobiotic metabolism in the inner zone of
the gland. N-terminal amino acid sequencing of the isolated protein re
vealed homology with members of the CYP2D subfamily. A human CYPD2D6 c
DNA probe was used to screen a guinea pig adrenal cDNA library and a f
ull-length clone was obtained having an open reading frame encoding a
500 amino acid protein. The sequence was found to be highly homologous
with all members of the CYP2D subfamily and was designated CYP2D16. T
he N-terminal sequence of 38 amino acids obtained from the protein mic
rosequencing was identical to that deduced from the nucleotide sequenc
e of the cloned CYP2D16. Northern blot analysis confirmed that CYP2D16
is expressed at high levels in the inner zone of the guinea pig adren
al cortex. The results suggest that CYP2D 16 may account, at least in
part, for the high rates of xenobiotic metabolism in the guinea pig ad
renal. (C) 1995 Acadenic Press, Inc.