ID JOS-BPB37_b13-00876
著者:名前 著者:別形式 Tamura, Mayumi / Watanabe, Tomoe / Igarashi, Takanori / Takeuchi, Tomoharu /Kasai, Ken-ichi / Arata, Yoichiro
著者:カナ 著者:所属 城西大学薬学部 / 城西大学薬学部 / 帝京大学薬学部 / 城西大学薬学部 / 帝京大学薬学部 / 城西大学薬学部
著者:所属(別形式) Josai University, Faculty of Pharmaceutical Sciences / Josai University, Faculty of Pharmaceutical Sciences / Teikyo University, School of Pharmaceutical Sciences, Department of Biological Chemistry / Josai University, Faculty of Pharmaceutical Sciences / Teikyo University, School of Pharmaceutical Sciences, Department of Biological Chemistry / Josai University, Faculty of Pharmaceutical Sciences
著者版フラグ publisher
出版地 東京
出版者 日本薬学会
出版者:カナ ニホンヤクガクカイ
出版者:別名 The Pharmaceutical Society of Japan
NCID AA10885497
冊子ISSN 09186158
電子ISSN 13475215
掲載誌名 巻 37
号 5
刊行年月 2014-05
開始ページ 877
終了ページ 882
コンテンツ作成日 2014-02-23
コンテンツ登録日 2014-11-08
識別番号:DOI info:doi/10.1248/bpb.b13-00876
識別番号:DOI(リンク) 識別番号:その他 JOI:DN/JST.JSTAGE/bpb/b13-00876
抄録 Galectins are a group of animal lectins characterized by their specificity for β-galactosides. In our previous study, we showed that a human galectin-1 (hGal-1) mutant, in which a cysteine residue was introduced at Lys28, forms a covalently cross-linked complex with the model glycoprotein ligands asialofetuin and laminin by using the photoactivatable sulfhydryl reagent benzophenone-4-maleimide (BPM). In the present study, we used several hGal-1 mutants in which single cysteine residues were introduced at different positions and examined their ability to form a covalent complex with asialofetuin or laminin by using BPM. We found that the efficiency of formation of the cross-linked products differed depending on the positions of the cysteine introduced and also on the ligand used for crosslinking. Therefore, by using different cysteine hGal-1 mutants, the chances of isolating different ligands for hGal-1 should increase depending on the systems and cells used.
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権利 Copyright c2014 The Pharmaceutical Society of Japan
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