Colorimetric assay for evaluating glycosyl fluoride-hydrolyzing activity of glycosidase by using alizarin complexon reagent

Chemistry Letters

Volumn 36, Issue 1, 2007, Pages 16-17

  Shoda, Shin Ichiro ^a   Shintate, Keiko ^a   Ishihara, Masaki ^a   Noguchi, Masato ^a   Kobayashi, Atsushi ^a  

^a TOHOKU UNIVERSITY   (Japan)

Author keywords

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Indexed keywords

EID: 34247251975     PISSN: 03667022     EISSN: None     Source Type: Journal    
DOI: 10.1246/cl.2007.16     Document Type: Article

References (20)

1. 2 was reported in 1981. T. Mukaiyama, Y. Murai, S. Shoda, Chem. Lett. 1981, 431.
2. b) For review see: K. Toshima, Carbohydr. Res. 2000, 527, 15, and references cited therein.
3. S. Shoda, in Glycoscience, ed. by B. O. Fraser-Reid, K. Tatsuta, J. Thiem, Springer, Heidelberg, 2001, Vol. II, pp. 1465-1496.
4. S. Shoda, M. Fujita, S. Kobayashi, Trend. Glycosci. Glycotechnol 1998, 54, 279, and references cited therein.
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6. S. Kobayashi, K. Kashiwa, T. Kawasaki, S. Shoda, J. Am. Chem. Soc. 1991, 113, 3079.
7. L. F. Mackenzie, Q. P. Wang, R. A. Warren, S. G. Withers, J. Am. Chem. Soc. 1998, 120, 5583.
8. The hydrolysis reaction of a glycosyl fluoride can be monitored by use of a fluoride ion selective electrode. However, this technique has serious problem that cannot be operated with many samples simultaneously. G. Okada, D. S. Genghof, E. J. Hehre, Carbohydr. Res. 1979, 71, 287.
9. 4
10. R. Greenhalgh, J. P. Riley, Anal. Chim. Acta 1961, 25, 179.
11. H. Wada, H. Mori, G. Nakagawa, Anal. Chim. Acta 1985, 172, 297.
12. When the complex formation was carried out under higher concentration of citric acid or phosphoric acid, a considerable absorbance decrease was observed.
13. 5
14. H. L. Lai, L. G. Butler, B. Axelrod, Biochem. Biophys. Res. Commun. 1974, 60, 635.
15. D. E. Koshland, Biol. Rev. Cambridge Phil. Soc. 1953, 28, 416.
16. H. Okada, K. Tada, T. Sekiya, K. Yokoyama, A. Takahashi, H. Tohda, H. Kumagai, Y. Morikawa, Appl. Environ. Microbiol. 1998, 64, 555.
17. One unit of the activity was defined as the amount of enzyme liberating 1.0 μ.mol of fluoride ion per minute.
18. 3+ ALC method, and urea was used to deactivate the enzyme catalyst.
19. The kinetic parameters obtained by two kinds of reactions terminated by acetone and urea are almost the same within experimental errors. The considerably large error in case of acetone may be caused by the lack of accuracy in the liquid handling.
20. The enzymatic glycosylation of several glycosyl acceptors by using β-lactosyl fluoride as donor catalyzed by EG-III leads to an efficient synthesis of the corresponding lactosides, the detail of which will be reported elsewhere as a full paper.