title: Distribution of microsomal CO-binding chromophores and EROD activity in sea anemone tissues.
abstract: Our previous studies indicated that sea anemone microsomes contain cytochrome P450 (CYP) and have ethoxyresorufin O-dealkylation (EROD) activity. Other marine invertebrates have discrete organs which concentrate cytochromes P450, whereas cnidarians have evolved only to the tissue level of development. To examine the distribution of CYP in sea anemones, microsomes were prepared from the following tissue regions of two sea anemones, Anthopleura xanthogrammica: outer (heavy muscular wall), inner (imperfect and perfect mesentery, and retractor muscle), soft (digestive sac, gonads, and mesentery filaments), and tentacular (including algal/diatom symbiont). The cytochrome P450 content was distributed relatively evenly among the tissue regions. In contrast, the 418-nm CO-binding chromophore was approximately 10 times greater in the outer region than in any other region. Further, the 490-nm peak (which interferes with quantification of CYP in sea anemones) was greater in the outer region. In general, the EROD activity was comparable in the inner and soft regions and highest in the tentacles. However, the EROD results may have been complicated by the presence of the algal/diatom symbiont.
authors.affiliation: Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA. herke@gateway.net
authors.forename: L M
authors.initials: LM
authors.lastname: Heffernan
authors.forename: G W
authors.initials: GW
authors.lastname: Winston
mesh_terms: D000818:Animals; D002248:Carbon Monoxide / Q000378:metabolism*; D019363:Cytochrome P-450 CYP1A1 / Q000378:metabolism*; D008861:Microsomes / Q000201:enzymology* / Q000648:ultrastructure; D010860:Pigments, Biological / Q000032:analysis* / Q000378:metabolism; D012615:Sea Anemones / Q000033:anatomy & histology / Q000201:enzymology* / Q000378:metabolism*; D013054:Spectrophotometry, Atomic / Q000662:veterinary
chemical_list: D010860:Pigments, Biological; D002248:Carbon Monoxide; D019363:Cytochrome P-450 CYP1A1