Respected readers, authors and reviewers, you can add comments to this page on any questions about the contribution, review, editing and publication of this journal. We will give you an answer as soon as possible. Thank you for your support!
ZHANG Di, LIN Yong, YAN Xiao-qin, LIAO Jian-hua, ZEN Hui, LIU Yan-ru. Extraction and Partial Characterization of A Lectin from Agaricus bisporus Strain AS2796[J]. Fujian Journal of Agricultural Sciences, 2011, 26(3): 457-461.
Citation:
ZHANG Di, LIN Yong, YAN Xiao-qin, LIAO Jian-hua, ZEN Hui, LIU Yan-ru. Extraction and Partial Characterization of A Lectin from Agaricus bisporus Strain AS2796[J]. Fujian Journal of Agricultural Sciences, 2011, 26(3): 457-461.
ZHANG Di, LIN Yong, YAN Xiao-qin, LIAO Jian-hua, ZEN Hui, LIU Yan-ru. Extraction and Partial Characterization of A Lectin from Agaricus bisporus Strain AS2796[J]. Fujian Journal of Agricultural Sciences, 2011, 26(3): 457-461.
Citation:
ZHANG Di, LIN Yong, YAN Xiao-qin, LIAO Jian-hua, ZEN Hui, LIU Yan-ru. Extraction and Partial Characterization of A Lectin from Agaricus bisporus Strain AS2796[J]. Fujian Journal of Agricultural Sciences, 2011, 26(3): 457-461.
A lectin was extracted and purified from the fruiting bodies of Agaricus bisporus strain 2796.The procedures included PBS extraction followed by precipitation with 40%-60%(NH4)2SO4 and filtration with DEAE-Sepharose fast flow ion-exchange chromatography and Sephadex G-100 gel filtration chromatography.The purified protein showed a band in SDS-PAGE with the subunit molecular weight of 15.7kDa.The relative molecular mass of the AS2796 lectin was 64.1kDa,as determined by the gel filtration on a Sephadex G-100 column.Four different isoelectric forms with pIs of 6.62,5.92,5.69 and 5.57 were separated by IEF-PAGE.The AS2796 lectin was stable under high temperatures.Its agglutinating activity did not decline significantly after heating at 80℃ for 10 minutes,and maintained at high level at pH 3.0-10.0.In addition,the activity was not found to be divalent metal ion-dependent.