A continuous fluorescence assay of renin activity

Analytical Biochemistry

Volumn 210, Issue 2, 1993, Pages 351-359

  Wang, Gary T ^a   Chung, Christine C ^a   Holzman, Thomas F ^a   Krafft, Grant A ^a  

^a ABBOTT LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENERGY TRANSFER; ENZYMES; EXCITED STATES; FLUORESCENCE; FLUORESCENCE QUENCHING; PEPTIDES; PH; PHYSIOLOGICAL MODELS; PROTEOLYSIS; QUENCHING;

96-WELL MICROTITER PLATE; CONCENTRATION LEVELS; CONTINUOUS FLUORESCENCE; EXCITED STATE LIFETIMES; FLUORESCENCE INTENSITIES; PROTEOLYTIC ACTIVITIES; RESONANCE ENERGY TRANSFER; SUBSTRATE INHIBITION;

FLUOROPHORES;

EID: 0027289345     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.1993.1207     Document Type: Article

References (35)

1. Laragh, J. H. (1986) J. Hypertension 4, S143
2. Reid, I. A. (1985) Arch. Intern. Med. 145, 1475
3. Laragh, J. H. (1985) J. Cardiovasc. Pharmacol 7, S86
4. Boger, J. (1985) in Annual Reports in Medicinal Chemistry (Bailey, D. M., and Egan, R. W.), Vol. 20, p. 257, Academic Press, New York
5. Brunner, H. R., et al. (1972) N. Engl. J. Med. 286, 441
6. Brunner, H. R., et al. (1973) Am. J. Med. 55, 295
7. Kaplan, N. M. (1975) J. Am. Med. Assoc. 231, 167
8. Alderman, M. H., et al. (1991) N. Engl. J. Med. 324, 1098
9. Haber, E., Koerner, T., Page, L. B., Kliman, B., and Purnode, A. (1969) J. Clin. Endocrinol. 29, 1349
10. Mendelsohn, F. A., and Colin, C. I. (1971) Biochem. J. 121, 241
11. Cimin, F., Le-Nguyen, D., Castro, B., Menard, J., and Corvol, J. P. (1987) Biochim. Biophys. Acta 913, 10
12. Reinhaez, A., and Roth, M. (1969) Eur. J. Biochem. 7, 334
13. Murakami, K., Ohsawa, T., Hirose, S., Takada, K., and Sakaki-bara, S. (1981) Anal. Biochem. 110, 232
14. Poorman, R. A., Palermo, D. P., Post, L. E., Murakami, K., Kin-ner, J. H., Smith, C. W., Reardon, I., and Heinrikson, R. L. (1986) Protein Structure Function, Genet. 1, 139
15. Matayoshi, E. D., Wang, G. T., Krafft, G. A., and Erickson, J. W. (1990) Science 247, 954-958
16. Wang, G. T., Matayoshi, E. D., Erickson, J. W., and Krafft, G. A. (1989) in Proceedings, Second International Conference on Drug Research in Immunologic and Infectious Diseases AIDS, Arlington, VA, Nov. 1989
17. Matayoshi, E. D., Wang, G. T., Kempf, D., Codacovi, L., and Erickson, J. W. (1989) in Proceedings, Second International Conference on Drug Research in Immunologic and Infectious Diseases, AIDS, Arlington, VA, Nov. 1989
18. Wang, G. T., Huffaker, J. A., Matayoshi, E. D., and Krafft, G. A. (1990) Tetrahedron Lett. 31, 6493-6496
19. Wang, G. T., Chung, C., Holzman, T. F., and Krafft, G. A. (1990) Biophys. J. 57, 39a
20. Holzman, T. F., Chung, C. C., Edalji, R., Egan, D. A., Gubbins, E. J., Reuter, A., Howard, G., Yang, L. K., Pederson, T. M., Krafft, G. A., and Wang, G. T. (1990) J. Protein Chem. 9, 663-672
21. Holzman, T. F., Chung, C. C., Edalji, R., Egan, D. A., Martin, M., Gubbins, E. G., Krafft, G. A., Wang, G. T., Thomas, A. M., Rosenberg, S. H., and Huchins, C. (1991) J. Protein Chem. 10, 553-563
22. Egan, D. A., Grzegorczyk, V., Tricarico, K. A., Reuter, A., Holle-man, W. H., and Marcotte, P. A. (1988) Biochim. Biophys. Acta 965, 68-75
23. E. Matayoshi, unpublished observations. This value was obtained from comparison of the equimolar fluorescence of free EDANS and Pro-Ile-Val-Gln-EDANS, the fluorescent hydrolysis product of the HIV protease substrate (15). It is assumed in this study that this value is also valid for Val-Ile-His-Thr-EDANS, the fluorescent hydrolytic fragment of the renin substrate
24. It should be emphasized that the calibration is certainly instrument dependent. Therefore, these results should not be applied to other instruments. The readers should perform their own calibration following the procedure outlined in this report
25. Latt, S. A., Auld, D. S., and Vallee, B. L. (1972) Anal. Biochem. 50, 56-62
26. Carmel, A., Zur, M., Yaron, A., and Katchalski, E. (1973) FEBS Lett. 30, 11-14
27. Presson, A., and Wilson, I. B. (1977) Anal. Biochem. 83, 296-303
28. Nishino, N., and Powers, J. (1980) J. Biol. Chem. 255, 3482-3486
29. Pohl, J., Davinic, S., Blaha, I., Strop, P., and Kostka, V. (1987) Anal. Biochem. 165, 96-101
30. Ng, M., and Auld, D. S. (1989) Anal. Biochem. 183, 50-56
31. Geoghegan, K. F., Spencer, R. W., Danley, D. E., Contillo, L. G., Jr., and Andrews, G. C. (1990) FEBS Lett. 262, 119-122
32. Tisljar, U., Knight, C. G., and Barrett, A. J. (1990) Anal. Biochem. 186, 112-115
33. Chagas, J. R., Juliano, L., and Prado, E. S. (1991) Anal. Biochem. 192, 419-425
34. Wathen, L. K., Nuorala, K. W., and Wathen, M. W. (1991) J. Clin. Lab. Anal. 5, 282
35. Oliveira, M. C. F., Hirata, I. Y., Chagas, J. R., Boschcov, P., Gomes, R. A. S., Figueiredo, A. F. S., and Juliano, L. (1992) Anal. Biochem. 203, 39