Mushroom Avidin

Avidin, a tetrameric glycoprotein from egg white, binds biotin (vitamin H) with remarkably high affinity; Streptavidin, an avidin-like protein from Streptomyces avidinii, also binds biotin strongly; Mushroom avidin is derive from mushroom (Pleurotus cornucopiae), and is a fungal avidin-like protein that binds biotin with high affinity. A drawback specific to avidin is its high level of non-specific binding to various biological components at physiological pH. Mushroom avidin shows a remarkably high affinity for biotin, like avidin and streptavidin. Mushroom avidin is a tetrameric protein and each subunit binds biotin with high affinity. It has higher thermo stability than those of avidin and streptavidin, and shows less nonspecific binding than avidin. The isoelectric point of Mushroom avidin is 7.4, lower than avidin (10.0), and slightly higher than that of streptavidin (6.0-7.5). The Tm (temperature of half-life period of biotin binding activity after heat treatment) value of Mushroom avidin is 85¡æ, higher than avidin from egg (79¡æ) and streptavidin (74¡æ). The Mushroom avidin - biotin interaction is widely employed as a universal tool in numerous biotechnological applications. For example, like avidin, it can be applied for affinity chromatography, ELISA, immunohistochemistry and Western Blotting, an so on.