{"refrec":{"BRefID":64702,"RR":"<b>Trainer, V.L.; Bill, B.D.</b> (2004). Characterization of a domoic acid binding site from Pacific razor clam. <i>Aquat. Toxicol. 69(2)</i>: 125-132. <a href=\"https://dx.doi.org/10.1016/j.aquatox.2004.04.012\" target=\"_blank\">https://dx.doi.org/10.1016/j.aquatox.2004.04.012</a>","BEntID":61187,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Aquat. Toxicol. 69(2)</i>: 125-132. <a href=\"https://dx.doi.org/10.1016/j.aquatox.2004.04.012\" target=\"_blank\">https://dx.doi.org/10.1016/j.aquatox.2004.04.012</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Trainer, V.L.; Bill, B.D.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Trainer, V.L.; Bill, B.D.","Englishabstract":"The Pacific razor clam, <i>Siliqua patula</i>, is known to retain domoic acid, a water-soluble glutamate receptor agonist produced by diatoms of the genus <i>Pseudo-nitzschia</i>. The mechanism by which razor clams tolerate high levels of the toxin, domoic acid, in their tissues while still retaining normal nerve function is unknown. In our study, a domoic acid binding site was solubilized from razor clam siphon using a combination of Triton X-100 and digitonin. In a Scatchard analysis using [<sup>3</sup>H]kainic acid, the partially-purified membrane showed two distinct receptor sites, a high affinity, low capacity site with a K<sub>D</sub> (mean ± S.E.) of 28 ± 9.4 nM and a maximal binding capacity of 12 ± 3.8 pmol/mg protein and a low affinity, high capacity site with a mM affinity for radiolabeled kainic acid, the latter site which was lost upon solubilization. Competition experiments showed that the rank order potency for competitive ligands in displacing [<sup>3</sup>H]kainate binding from the membrane-bound receptors was quisqualate > ibotenate > IODOWILLARDIINE = AMPA = fluorowillardiine > domoate > kainate > -glutamate. At high micromolar concentrations, NBQX, NMDA and ATPA showed little or no ability to displace [<sup>3</sup>H]kainate. In contrast, Scatchard analysis using [<sup>3</sup>H]glutamate showed linearity, indicating the presence of a single binding site with a K<sub>D</sub> and B<sub>max</sub> of 500 ± 50 nM and 14 ± 0.8 pmol/mg protein, respectively. These results suggest that razor clam siphon contains both a high and low affinity receptor site for kainic acid and may contain more than one subtype of glutamate receptor, thereby allowing the clam to function normally in a marine environment that often contains high concentrations of domoic acid.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Characterization of a domoic acid binding site from Pacific razor clam","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-06-10 01:31:27.457305","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"domoic acid; kainic acid; razor clam; glutamate receptor; kamate bindingprotein; receptor binding","OtherDescriptors":"Domoic acid; Kainic acid; Razor clam; Glutamate receptor; Kainate binding protein; Receptor binding","Notes":null,"AnaPub":2004,"MonPub":null,"DateUpdate":"2020-10-02","DateCreate":"2004-08-03","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000223021200002","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.aquatox.2004.04.012"},"refs":null,"anarec":{"AnaID":64702,"PubliDate":2004,"Pagination":"125-132","XtraPublOfAnaID":null,"ISBN":null,"Volume":"69","Issue":"2","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42203,"SerRR":"Aquatic Toxicology. Elsevier Science: Tokyo; New York; London; Amsterdam.  ISSN 0166-445X; e-ISSN 1879-1514","StandardTitleSer":"Aquatic Toxicology","ISSN":"0166-445X","AbbrevSer":"Aquat. 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