An acid-tolerant lectin coupled with high Hg2+ potentiated hemagglutination enhancing property purified from Amanita hemibapha var. ochracea
文献类型： 外文期刊
作者： Sekete, Malota 2 ; Ma, Duanzheng 1 ; Wang, Bo 4 ; Wang, He Xiang 1 ; Gong, Zhiyuan 5 ; Ng, Tzi Bun 6 ;
作者机构： 1.China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China
2.China Agr Univ, Dept Microbiol, Beijing 100193, Peoples R China
3.Minist Agr & Food Secur, Agr Res Dept, Mushroom Res Unit, Maseru 100, Lesotho
4.Sichuan Acad Agr Sci, Soil & Fertilizer Inst, Chengdu 610066, Sichuan, Peoples R China
5.Shandong Acad Agr Sci, Inst Agr Resources & Environm, Jinan 250100, Shandong, Peoples R China
6.Chinese Univ Hong Kong, Fac Med, Sch Biomed Sci, Shatin, Hong Kong, Peoples R China
关键词： Purification; Mushroom; Lectin; Amanita; Agglutination
期刊名称：PROCESS BIOCHEMISTRY （ 影响因子：3.757； 五年影响因子：3.665 ）
ISSN： 1359-5113
年卷期： 2014 年 49 卷 3 期
页码：
收录情况： SCI
摘要： A 37.4 kDa acid tolerant lectin was isolated and purified from dried fruiting bodies of Amanita hemibapha var. ochracea designated as AHL. The lectin was not adsorbed on DEAE-cellulose, but rather adsorbed on S-Sepharose and subjected to gel filtration by fast protein liquid chromatography on Superdex 75. The purified lectin was immune from inhibition activities of metal ions. More over, AHL exhibited high agglutination activity on rabbit erythrocytes with accelerating Hg2+ ions concentration. Partial peptide sequence analysis (VSNNLLTGPKVVR) of this lectin showed relative similarity to phosphoenolpyruvate carboxykinase [ATP]-like protein as predicted from Fragaria vesca subsp. Vesca. Interestingly, AHL displayed a strong affinity toward alpha-Lactose, making our study the first report associating Amanita species' lectin specificity for alpha-Lactose to the best of our knowledge. (C) 2014 Elsevier Ltd. All rights reserved.
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