Zeltins A, Schrempf H
FB Biologie/Chemie, Universität Osnabrück, Germany.
Anal Biochem. 1995 Nov 1;231(2):287-94. doi: 10.1006/abio.1995.0053.
Recently we identified a so far unique protein (CHB1) which interacts specifically with crystalline alpha-chitin. Having optimized the binding conditions for CHB1 coupled with fluorescein isothiocyanate (FITC), we succeeded in developing a highly sensitive assay to detect alpha-chitin. CHB1-FITC interacted neither with beta- or colloidal chitin nor with chitooligomers or cellulose. With the help of fluorescence or confocal laser microscopy, the relative location of crystalline alpha-chitin within various native samples of fungi and other organisms can be clearly and rapidly visualized.
最近,我们鉴定出一种迄今为止独一无二的蛋白质(CHB1),它能与结晶α-几丁质特异性相互作用。在优化了CHB1与异硫氰酸荧光素(FITC)偶联的结合条件后,我们成功开发出一种高灵敏度检测方法来检测α-几丁质。CHB1-FITC既不与β-几丁质或胶体几丁质相互作用,也不与壳寡糖或纤维素相互作用。借助荧光或共聚焦激光显微镜,可以清晰、快速地观察到结晶α-几丁质在各种真菌和其他生物体天然样本中的相对位置。