{"refrec":{"BRefID":281152,"RR":"<b>Lamy, J.; Gielens, C.; Lambert, O.; Taveau, J.C.; Motta, G.; Loncke, P.; Degeest, N.; Preaux, G.</b> (1993). Further approaches to the quaternary structure of <i>Octopus</i> hemocyanin: a model based on immunoelectron microscopy and image processing. <i>Arch. Biochem. Biophys. 305(1)</i>: 17-29. <a href=\"https://dx.doi.org/10.1006/abbi.1993.1388\" target=\"_blank\">https://dx.doi.org/10.1006/abbi.1993.1388</a>","BEntID":273171,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Arch. Biochem. Biophys. 305(1)</i>: 17-29. <a href=\"https://dx.doi.org/10.1006/abbi.1993.1388\" target=\"_blank\">https://dx.doi.org/10.1006/abbi.1993.1388</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Lamy, J.; Gielens, C.; Lambert, O.; Taveau, J.C.; Motta, G.; Loncke, P.; Degeest, N.; Preaux, G.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Lamy, J. <i>et al.</i>","Englishabstract":"The direction of the potypeptide chains and the location of the functional units in <i>Octopus vulgaris</i> hemocyanin were studied by various methods. Monoclonal antibodies specific for the <i>Ovc</i> (clone Ov409) and <i>Ovg</i> (clone Ov315) functional units produced immunocomplex strings which were examined in the electron microscope. In both cases the immunocomplexes contained more than two hemocyanin molecules in their side view, demonstrating that in the whole hemocyanin neighboring polypeptide chains run in antiparallel directions. The interhemocyanin distances in the immunocomplexes also indicated that <i>Ovg</i> is located inside the cylinder, while <i>Ovc</i> is located in the external layers of functional units. In addition, the fact that the binding point of the Fab arm to the hemocyanin molecule was occasionally visible confirmed the external location of functional unit <i>Ovc</i>. Image processing of the whole hemocyanin cross-linked with dimethyl suberimidate showed that the end-on view is not a perfect cylinder but a regular pentahedron and that the five-arch collar is probably composed of five pairs of functional unit <i>Ovg</i> located inside the cylinder. The accessibility of cross-linked hemocyanin to functional unit-specific polyclonal antibodies, studied in immunoelectrophoresis, showed that <i>Ovb</i> and <i>Ove</i> are highly accessible, while <i>Ovd</i>, <i>Ovf</i>, and <i>Ovg</i> are not. The low accessibility of <i>Ovd</i> may be at least partially explained by its high sugar content which could hamper the accessibility of the antibody to the antigen.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Further approaches to the quaternary structure of <i>Octopus</i> hemocyanin: a model based on immunoelectron microscopy and image processing","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-06-10 01:32:03.788468","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":1993,"MonPub":null,"DateUpdate":"2022-04-13","DateCreate":"2016-10-12","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:A1993LT02400003","VABBcode":null,"OpenAcc":0,"DOI":"10.1006/abbi.1993.1388"},"refs":null,"anarec":{"AnaID":281152,"PubliDate":1993,"Pagination":"17-29","XtraPublOfAnaID":null,"ISBN":null,"Volume":"305","Issue":"1","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42387,"SerRR":"Archives of biochemistry and biophysics. 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