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
Identifiers and Pagination:Year: 2011
First Page: 78
Last Page: 82
Publisher Id: TOMSJ-5-78
Article History:Received Date: 28/9/2010
Revision Received Date: 5/11/2010
Acceptance Date: 22/12/2010
Electronic publication date: 02/5/2011
Collection year: 2011
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: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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).