An acid-tolerant lectin coupled with high Hg2+ potentiated hemagglutination enhancing property purified from Amanita hemibapha var. ochracea |
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| Institution: | 1. Department of Obstetrics and Gynecology, Nnamdi Azikiwe University Teaching Hospital, Nnewi, Nigeria;2. Department of Community Medicine, Nnamdi Azikiwe University Teaching Hospital, Nnewi, Nigeria;3. Department of Obstetrics and Gynecology, Anambra State University Teaching Hospital, Awka, Nigeria;4. Department of Obstetrics and Gynecology, Michigan State University/Sparrow Hospital, Lansing, USA;1. Department of Biomedical Science, Daegu University, Gyeongsan 712-714, South Korea;2. School of Life Sciences and Biotechnology, Kyungpook National University, Daegu 702-701, South Korea;3. Center for Bio-Nanomaterials, Daegu University, Gyeongsan 712-714, South Korea |
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| Abstract: | 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 α-Lactose, making our study the first report associating Amanita species’ lectin specificity for α-Lactose to the best of our knowledge. |
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| Keywords: | Purification Mushroom Lectin Amanita Agglutination |
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