An acid-tolerant lectin coupled with high Hg2+ potentiated hemagglutination enhancing property purified from Amanita hemibapha var. ochracea

Autor:	Duanzheng Ma, Zhiyuan Gong, Bo Wang, Tzi Bun Ng, He Xiang Wang, Malota Sekete
Rok vydání:	2014
Předmět:	Amanita biology Hemagglutination Lectin Bioengineering Fast protein liquid chromatography biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Agglutination (biology) Amanita hemibapha biology.protein Phosphoenolpyruvate carboxykinase Peptide sequence
Zdroj:	Process Biochemistry. 49:535-539
ISSN:	1359-5113
Popis:	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 Hg 2+ 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::3b6aeb4e96c89ccef0c279a8f8e45224 https://doi.org/10.1016/j.procbio.2013.11.011 Zobrazit plný text záznamu Full Text from ScienceDirect