INTERACTION BETWEEN THE SURFACE GLYCOSYLATED POLYPROPYLENE MEMBRANE AND LECTIN

Qian Yang; Ling-shu Wan; Zhi-kang Xu

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INTERACTION BETWEEN THE SURFACE GLYCOSYLATED POLYPROPYLENE MEMBRANE AND LECTIN

Note | Updated：2021-06-21

- INTERACTION BETWEEN THE SURFACE GLYCOSYLATED POLYPROPYLENE MEMBRANE AND LECTIN
- Vol. 26, Issue 3, Pages: 363-367(2008)
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- Published：20 May 2008
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Qian Yang, Ling-shu Wan, Zhi-kang Xu. INTERACTION BETWEEN THE SURFACE GLYCOSYLATED POLYPROPYLENE MEMBRANE AND LECTIN[J]. 2008, 26(3): 363-367.
DOI：

Qian Yang, Ling-shu Wan, Zhi-kang Xu. INTERACTION BETWEEN THE SURFACE GLYCOSYLATED POLYPROPYLENE MEMBRANE AND LECTIN[J]. 2008, 26(3): 363-367. DOI：

摘要

A glycopolymer bearing glucose residues was tethered onto the surface of polypropylene microporous membrane by UV-induced graft polymerization of α-allyl glucoside. Concanavalin A (Con A)

a glucose recognizing lectin

could be specifically adsorbed to the membrane surface. On the other hand

the membrane surface showed no recognition ability to another lectin peanut agglutinin. Moreover

the recognition complex between the glycosylated membrane surface and Con A could be inhibited by glucose and mannose solution. This surface glycosylated membrane could be used as affinity membrane for protein separation and purification.

Abstract

A glycopolymer bearing glucose residues was tethered onto the surface of polypropylene microporous membrane by UV-induced graft polymerization of α-allyl glucoside. Concanavalin A (Con A)

a glucose recognizing lectin

could be specifically adsorbed to the membrane surface. On the other hand

the membrane surface showed no recognition ability to another lectin peanut agglutinin. Moreover

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