{"_buckets": {"deposit": "e4611859-b09b-4f82-9c0c-766be492a478"}, "_deposit": {"created_by": 4, "id": "5065", "owners": [4], "pid": {"revision_id": 0, "type": "depid", "value": "5065"}, "status": "published"}, "_oai": {"id": "oai:az.repo.nii.ac.jp:00005065", "sets": ["262", "494"]}, "author_link": ["21988", "21992", "21990", "21989", "21993", "21991"], "item_12_biblio_info_16": {"attribute_name": "書誌情報", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "2008-03-31", "bibliographicIssueDateType": "Issued"}, "bibliographicPageEnd": "276", "bibliographicPageStart": "274", "bibliographicVolumeNumber": "15/16", "bibliographic_titles": [{"bibliographic_title": "麻布大学雑誌"}, {"bibliographic_title": "Journal of Azabu University", "bibliographic_titleLang": "en"}]}]}, "item_12_description_13": {"attribute_name": "抄録", "attribute_value_mlt": [{"subitem_description": "条虫から,生体膜上で集合してできると考えられている微小膜領域である膜ミクロドメインを調製し,糖脂質およびタンパク質糖鎖について実験を行った結果,低密度であるDIGs画分にAK97に反応する精脂質および精タンパクが局在していることがわかった。インフルエンザウイルスやヒト免疫不全ウイルス(HIV)の感染には精鎖が重要な役割を担うことが知られており,精鎖は条虫類の感染にも深く関与している可能性は極めて高く,固有宿主と非固有宿主を識別する因子として精脂質や精タンパク質のさらなる実験が必要であると考えられた。", "subitem_description_type": "Abstract"}]}, "item_12_description_14": {"attribute_name": "Abstract", "attribute_value_mlt": [{"subitem_description": "Detergent-insoluble glycolipid-enriched complexes (DIGs) formed as microdomains in the cell membranes have been shown to contain signalling molecules, cholesterol, glycosphingolipids and caveolae. DIGs can be expected to be involved in the mediation of host-parasite interactions. In this context, we have been studying DIGs of cestodes to elucidate underlying biochemical mechanisms of parasitism. We previously reported unique Glycosphingolipids, SEGLx and GalSEGLx, from the Pseudophyllidean tapeworms (Spirometra erinaceieuropaei). They were characterized by a carbohydrate structure Galβ1-4Glcβ-3Gal. We proposed a term \"spirometosides\" for glycolipids having this core (Kawakami et al. Eur. J. Biochem. 1996; 239; 905-11) and we also successively established a mouse monoclonal IgM antibody directed to SEGLx, and termed AK97 (Yanagisawa et al. Mol Biochem Parasitol. 1999; 102; 285-297). In this study, we analyzed worm proteins in DIG by western blotting using AK97. Fraction 6 and Fraction 7 were reacted with AK97. As anticipated, glycilipids were also present same fractions. 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