Purification and Identification of a Natural Lectin from the Seed of Peanut Arachis hypogaea

Jie Sun*, Qing-li Yang, jie Bi, Chu-shu Zhang, Li-na Yu, Feng Zhu
Shandong Peanut Research Institute, Fushan Road No. 126, Licang District, Qingdao 266100, China.

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© 2011 Sun et al;

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

* Address correspondence to this author at the Shandong Peanut Research Institute, Fushan Road No. 126, Licang District, Qingdao 266100, China; Tel: +86-532-87611087; Fax: +86-532-87611087; E-mails:,


A natural lectin from the seed of peanut Arachis hypogaea was purified by singlestep affinity chromatography using galactoside-coupled agarose. The native molecular mass of purified A. hypogaea lectin (PN-L) was 29 kDa. The lectin PN-L was detected for agglutinating activity, glycoinhibiting action and thermostability. The influence of pH on those activities was also tested. The results showed that PN-L could not agglutinate three kinds of human erythrocytes. But it showed a strong affinity to human A, B and O erythrocytes (RBC) treated by neuraminidase. Agglutinating activity of PN-L to neuraminidase treated human O erythrocytes was inhibited by lactose, raffinose, melibiose and D-galactose. The agglutinating activity of peanut seed lectin was stable up to 55°C and at pH 5.0-11.0. The results of MALDI-TOFTOF analysis indicated that the protein PN-L showed highly homology with the Peanut Lectin Chain A protein (gi|1942899).

Keywords: Peanut, lectin, agglutinating activity, property.