This is an example of a CDA polymorphism characterized experimentally by using a microsome and fluorescent and non-fluorescent dyes. The polymorphism is known to exist in many of the mammalian species. A CDA-1 genotype was shown to be associated with high serum acetaminophen levels, with a CDA genotype at the extreme low end of the normal pattern of variability of this enzyme in humans. The CDA allele was also demonstrated to have a deleterious impact on the function of various enzymes in various regions of the body. The polymorphism is not completely penetrant. The presence of a non-functional CDA may be caused by mutation or translocation of the gene or by disruption of the methylation process (Methylation of the CDA gene is affected by the CDA -1 allele, whereas Methylation is unaffected by the common C1 allele). The polymorphism may affect only a subset of Caucasians but has been demonstrated to be heterogeneous in Japanese, Caucasian, African, and Asian populations. Keywords. Alcohol, Clostridium septum, Caffeine, Clotting, Coding/Coding DNA, Enzymes, Genotype, Methylation, Nonspecific, Pharmacokinetics, Polymorphism. In 1992, the Pharmacokinetics Branch, U.S. Food and Drug Administration (FDA) reported the results of a study examining the pharmacophore of the clostridium septum alpha-glucocerebrosus (CLC) C-32 gene (Hennighausen et al., Lancet, May 31, 1992, pp.). This study was to determine if a polymorphism of the gene coding for the alpha-galactosyltransferase (alpha-gal) enzyme with a T to G transition on the second exon had any impact on drug concentrations in plasma. The CLC C-32 gene is an algal gene. The CLC gene has two exons, with one exon coding for the alpha-gal gene with two exons. The CLC gene is transcribed in the first exon, and the gene products are encoded in the second exon.
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Pro. Neill. Acid. Sci. USA Vol. 89, pp. 1685-1689, March 1992 Biochemistry Molecular cloning of the flavin-containing monooxygenase (form II) CDA from adult human liver (mammalian amine/sulfide oxygenate/Ziegler's
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