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

Voelter, W. and Wacker, R. and Franz, M. and Maier, T. and Stoeva, S.. (2000) Complete structural characterization of a chitin-binding lectin from mistletoe extracts. Journal für praktische Chemie, 342 (8). pp. 812-818.

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From mistletoe extracts, a chitin-binding lectin (cbML) was isolated and its primary structure determined. The protein is composed of two identical protein chains, linked by am interchenary disulfide bond. Each chain is characterized by four intrachenary disulfide bridges. The structure shows high homology to hevein, one of the prominent allergens of natural rubber latex. cbML could also be detected in commercially available pharmaceutical mistletoe extract preparations. The described isolation procedure and characterization allows isolation of cbML in highly pure form and sufficient quantities, now ready for unequivocal determination for its pharmacological effects.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
UniBasel Contributors:Maier, Timm
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:03 Nov 2017 09:50
Deposited On:03 Nov 2017 09:50

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