Visualization of α-Chitin with a Specific Chitin-Binding Protein (CHB1) fromStreptomyces olivaceoviridis
✍ Scribed by Andris Zeltins; Hildgund Schrempf
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 252 KB
- Volume
- 231
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
presence of chitin, but not its relative location within Recently we identified a so far unique protein tissues.
(CHB1) which interacts specifically with crystalline a-
The lectin wheat germ agglutinin (WGA) 2 recognizes chitin. Having optimized the binding conditions for a sequence of three N-acetylglucosamine residues. CHB1 coupled with fluorescein isothiocyanate (FITC), Therefore it has a strong affinity for the oligomers and we succeeded in developing a highly sensitive assay polymers of this sugar (7). It is possible to detect the to detect a-chitin. CHB1-FITC interacted neither with binding of WGA by immunofluorescence using antibodb-or colloidal chitin nor with chitooligomers or celluies raised against WGA or WGA coupled with a fluolose. With the help of fluorescence or confocal laser rescent dye (8,9). Recently, we discovered that Streptomicroscopy, the relative location of crystalline a-chimyces olivaceoviridis secretes a so far unique 18.7-kDa tin within various native samples of fungi and other protein (CHB1) which specifically binds to a-chitin. The organisms can be clearly and rapidly visualized. protein was purified to homogeneity, and its gene was