@article{oai:tohoku-mpu.repo.nii.ac.jp:00000021,
 author = {細野, 雅祐 and Hosono, Masahiro and 村上, 奈緒 and Murakami, Nao and 高松, 友里絵 and Takamatsu, Yurie and 菅原, 栄紀 and Sugawara, Shigeki and 立田, 岳生 and Tatsuta, Takeo and 仁田, 一雄 and Nitta, Kazuo},
 issue = {59},
 journal = {東北薬科大学研究誌, Journal of Tohoku Pharmaceutical University},
 month = {Dec},
 note = {Fish eggs or roe often contain rhamnose-binding lectins (RBLs) that have unique properties among animal lectins in the carbohydrate recognition and domain structure. To investigate new lectin activity in deep-sea fishes,we attempted to extract proteins from eggs (GFE) and liver (GFL) of goose fish,Lophius litulon. The crude saline-extracted fraction (SEF) was obtained from acetone-dried powders of GFE and GFL.Each SEF was separated by DEAE-ion exchange chromatography. Contrary to our expectation,any DEAE fractions had no hemaggulatination activity on rabbit erythrocytes. On the other hand,S-180 mouse ascites tumor cells were strongly aggutinated by GFL D100,D200 and SC fractions with the final concentrations required minimum agglutination,65.0, 98.75 and 112.5ug/mL,respectively. Whereas any typical ligand molecules including carbohydrates and glycoconjugates showed no inhibitory effect for such tumor cell agglutination,several protease inhibitors including phenylmethanesufonyl fluoride and EDTA could do that. agglutination was caused by their proteolytic activity on the tumor cell surface components.The results from additional separation by hydroxyapatite column chromatography,SDS-PAGE and zymography indicated that putative candidates possessing proteolytic activity might be ca. 100 or 45 kDa proteins.},
 pages = {51--57},
 title = {キアンコウ(Lophius litulon)におけるレクチン活性の探索},
 year = {2012},
 yomi = {ホソノ, マサヒロ and ムラカミ, ナオ and タカマツ, ユリエ and スガワラ, シゲキ and タツタ, タケオ and ニッタ, カズオ}
}