Competitive inhibitory effects of acetazolamide upon interactions with bovine carbonic anhydrase II

Protein Journal

Volumn 26, Issue 6, 2007, Pages 371-385

  Safarian, Shahrokh ^a   Bagheri, Fatemeh ^a   Moosavi Movahedi, Ali Akbar ^a   Amanlou, Massoud ^b   Sheibani, Nader ^c  

^a UNIVERSITY OF TEHRAN   (Iran)

^b TEHRAN UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^c UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

Acetazolamide; Binding study; Bovine carbonic anhydrase II; Competitive inhibition; Isoforms

Indexed keywords

ACETAZOLAMIDE; AMINO ACID; CARBONATE DEHYDRATASE; CARBONATE DEHYDRATASE II; IODIDE ION; ISOENZYME; TRYPTOPHAN;

ARTICLE; BINDING SITE; CATALYSIS; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CYTOSOL; DRUG PROTEIN BINDING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INACTIVATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; FLUORESCENCE; KINETICS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; THERMOSTABILITY; ULTRAVIOLET RADIATION;

BOVINAE;

EID: 34548413624     PISSN: 15723887     EISSN: 18758355     Source Type: Journal    
DOI: 10.1007/s10930-007-9073-4     Document Type: Article

References (34)

1. Abbate F., Casini A., Scozzafava A., Supuran C. T. (2004) Bioorg. Med. Chem. Lett. 14:2357-2361
2. Agrawal V. K., Bano S., Supuran C. T., Khadikar P. V. (2004) Eur. J. Med. Chem. 39:593-600
3. Armstrong J. M., Meyrs D. V., Verpoorte J. A., Edsall J. T. (1966) J. Biol. Chem. 241:5137-5149
4. Bardsley W. G., Leff P., Kavanagh, J., Waight R. (1980) Biochem. J. 187:739-765
5. Bohm G., Muhr R., Jaenicke R. (1992) Protein Eng. 5:191-195
6. Burnham L., Dollimore D., Alexander K. S. (2001) Themochimica Acta, 392:127-134
7. Chakravarty S., Kannan K. K. (1994) J. Mol. Biol. 243:298-309
8. Coleman J. E. (1967) J. Biol. Chem. 242:5212-5219
9. Freifilder D. (1985) Physical Chemistry with Application to Biological Science. Jones and Bartlett Publishers, Inc, Bostone, MA
10. Hakansson K., Carlsson M., Svensson L. A., Lilijas A. (1992) J. Mol. Biol. 227:1192-1204
11. Hinz H. J. (1983) Annu. Rev. Biophys. Bioeng. 12:258-317
12. Lindskog S. (1963) J. Biol. Chem. 238:945-951
13. Lindskog S. (1997) Pharmacol. Ther. 74:1-20
14. Lindskog S., Thorslund A. (1968) Eur. J. Biochem. 3:453-460
15. Liu L. P., Deber C. M. (1997) Biochemistry, 36:5476-5482
16. Moosavi-Movahedi Z., Safarian S., Zahedi M., Sadeghi M. Saboury A. A., Chamani J., Bahrami H., Ashraf-Modaress A., Moosavi-Movahedi A. A. (2006) Protein J. 25:193-201
17. Nyman P. O., Lindskog S. (1964) Biochim. Biophys. Acta 85:141-151
18. Ohta S. Alam M. T., Arakawa H., Ikai A. (2004) Biophys. J. 87:4007-4020
19. Pocker Y., Stone J. T. (1967) Biochemistry 6:668-678
20. Radhakrishnan R., Sluka K. A. (2005) J Pharmacol Exp Ther. 313:221-227
21. Richter A., Hamann M. (2004) Eur. J. Pharmacol. 502:105-108
22. Riehl B, Schlue W. R. (1993) Comp. Biochem. Physiol. B 106:717-718
23. Safarian S., Saffarzadeh M., Zargar S. J., Moosavi-Movahedi A. A. (2006) J. Biochem. (Tokyo) 139:1025-1033
24. Saito R., Sato T., Ikai A., Tanaka N. (2004) Acta Crystallogr. D. Biol. Crystallogr. 60:792-795
25. Sergienko E. A., Srivastava D. K. (1997) Biochem. J. 328:83-91
26. Shoichet B. K., Baase W. A., Kuroki R., Matthews B. W. (1995) Proc. Natl. Acad. Sci. U.S.A 92:452-456
27. Shrake A., Rupley J. A. (1973) J. Mol. Biol. 79:351-371
28. Supuran C. T., Scozzafava A. (2001) Curr. Med. Chem Imm. Endoc. Metab. Agents 1:61-97
29. Tashian R. E., Plato C. C., Shows T. B. (1963) Science 140:53-54
30. Thorslund A., Lindskog S. (1967) Eur. J. Biochem. 3:117-123
31. Vidgren J., Liljas A., Walker N. P. C. (1990) Int. J. Biol. Macromol. 12:342-344
32. Vidgren J., Svensson A., Liljas A. (1993) Int. J. Biol. Macromol. 15:97-100
33. Wimley W. C., Creamer T. P., White S. H. (1996) Biochemistry, 35:5109-5124
34. Wingard L. B., Brody T. M., Larner J., Schwartz A. (1991) Human Pharmacology: Molecular to Clinical. Mosby-Year Book, Inc, St. Louis, Missouri