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与山黧豆、兵豆和豌豆凝集素反应的单克隆抗体6,F-8的进一步特性分析

Further characterization of monoclonal antibody 6,F-8 reacting with Lathyrus, Lens and Pisum lectins.

作者信息

Kolberg J, Rougé P

机构信息

Department of Immunology, National Institute of Public Health, Oslo, Norway.

出版信息

FEBS Lett. 1989 Apr 10;247(1):77-80. doi: 10.1016/0014-5793(89)81244-x.

Abstract

The murine monoclonal antibody (MoAB) 6,F-8 made against the glucose/mannose-specific Lathyrus odoratus mitogen has previously been shown to react with Lens culinaris and Pisum sativum lectins, but not with the lectin from Vicia faba [(1988) Biol. Chem. Hoppe-Seyler 369, 365-370]. The reactivity against seven other completely sequenced Lathyrus lectins has now been tested after separation of the subunits by SDS-polyacrylamide gel electrophoresis and electroblotting to nitrocellulose filters. Two of these lectins reacted with the antibody. Comparison of the amino acid sequences of the examined lectins and the predicted hydrophilic, flexible and accessible regions of Pisum sativum suggest that valine-147 is involved in antibody binding.

摘要

先前已证明,针对葡萄糖/甘露糖特异性香豌豆属有丝分裂原制备的鼠单克隆抗体(MoAB)6,F-8可与兵豆凝集素和豌豆凝集素发生反应,但不与蚕豆凝集素发生反应[(1988年)《生物化学与霍佩-赛勒》369, 365 - 370]。在通过SDS - 聚丙烯酰胺凝胶电泳分离亚基并电印迹到硝酸纤维素滤膜上后,现已测试了该抗体与其他七种完全测序的香豌豆属凝集素的反应性。其中两种凝集素与该抗体发生了反应。对所检测凝集素的氨基酸序列以及豌豆预测的亲水性、柔性和可及区域进行比较表明,缬氨酸 - 147参与了抗体结合。

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