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  • Title: Monolayers assembled from a glycolipid biosurfactant from Pseudozyma (Candida) antarctica serve as a high-affinity ligand system for immunoglobulin G and M.
    Author: Imura T, Ito S, Azumi R, Yanagishita H, Sakai H, Abe M, Kitamoto D.
    Journal: Biotechnol Lett; 2007 Jun; 29(6):865-70. PubMed ID: 17342348.
    Abstract:
    A carbohydrate ligand system has been developed which is composed of self-assembled monolayers (SAMs) of mannosylerythritol lipid-A (MEL-A) from Pseudozyma antarctica, serving for human immunoglobulin G and M (HIgG and HIgM). The estimated binding constants from surface plasmon resonance (SPR) measurement were Ka = 9.4 x 10(6) M(-1) for HIgG and 5.4 x 10(6) M(-1) for HIgM, respectively. The binding site was not in the Fc region of immunoglobulin but in the Fab region. Large amounts of HIgG and HIgM bound to MEL-A SAMs were directly observed by atomic force microscopy.
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