Complete structural characterization of a chitin-binding lectin from mistletoe extracts

From mistletoe extracts, a chitin-binding lectin (cbML) was isolated and it s primary structure determined. The protein is composed of two identical pr otein chains, linked by am interchenary disulfide bond. Each chain is chara cterized by four intrachenary disulfide bridges. The structure shows high h omology to hevein, one of the prominent allergens of natural rubber latex. cbML could also be detected in commercially available pharmaceutical mistle toe extract preparations. The described isolation procedure and characteriz ation allows isolation of cbML in highly pure form and sufficient quantitie s, now ready for unequivocal determination for its pharmacological effects.