Isolation, Purification and Hemagglutination Property of Lectin from Allium chinense

doi:10.7506/spkx1002-6630-201319018

Abstract

Abstract:

Lectin from the bulb of Allium chinense (ACL) was isolated by extraction with phosphate buffer solution (pH 7.3),
precipitation by 80% (NH4)2SO4, and separation by Q Sepharose strong anion exchange chromatography and Superdex
200 HR 10/30 chromatography. In agglutination test, the minimum erythrocyte agglutination concentration of ACL
was 0.2 μg/mL, and the hemagglutinating activity was maintained even after heating at 70 ℃ for 10 min. The agglutination
activity declined after treated with 100 mmol/L NaOH but was stable in the presence of 100 mmol/L HCl, suggesting that
ACL is acid-stable but not alkali-stable. The hemagglutination of the lectin on rabbit erythrocytes was inhibited by mannose
among the tested sugars in this study, suggesting ACL to be a mannose binding lectin.

Key words: Allium chinense, lectin, purification, high performance liquid chromatography (HPLC), hemagglutination

CLC Number:

Q946

XIAO Xiu-qing，DING Xue-zhi*，XIA Li-qiu，YANG Qi，XU Sha. Isolation, Purification and Hemagglutination Property of Lectin from Allium chinense[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201319018.

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Isolation, Purification and Hemagglutination Property of Lectin from Allium chinense

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