Solution-active structural alterations in liganded hemoglobins C (β6 Glu → Lys) and S (β6 Glu→ Val)

Journal of Biological Chemistry

Volumn 274, Issue 20, 1999, Pages 13777-13782

  Hirsch, Rhoda Elison ^a   Juszczak, Laura J ^a   Fataliev, Nazim A ^a   Friedman, Joel M ^a   Nagel, Ronald L ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN; HEMOGLOBIN A; HEMOGLOBIN C; HEMOGLOBIN S;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CRYSTALLOGRAPHY; ERYTHROCYTE; FLUORESCENCE; HUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; RAMAN SPECTROMETRY; SPECTROSCOPY; STRUCTURE ANALYSIS;

AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; FLUOROMETRY; HEMOGLOBIN C; HEMOGLOBIN, SICKLE; HUMANS; OXYGEN; PROTEIN CONFORMATION; SOLUTIONS; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTRUM ANALYSIS, RAMAN;

EID: 0033553430     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.20.13777     Document Type: Article

References (59)

1. Hirsch, R. E., Lin, M. J., Vidugiris, G. V. A., Huang, S., Friedman, J. M., and Nagel, R. L. (1996) J. Biol. Chem. 271, 372-375
2. Hirsch, R. E., Rybicki, A. C., Fataliev, N. A., Lin, M. J., Friedman, J. M., and Nagel, R. L. (1997) Br. J. Haematol. 98, 583-588
3. Asakura, T., Agarwal, P. L., Relman, D. A., McCray, J. A., Chance, B., Schwartz, E., Friedman, S., and Lubin, B. (1973) Nature 244, 437-438
4. Asakura, T., Adachi, K., Sono, M., Friedman, S., and Schwartz, E. (1974) Biochem. Biophys. Res. Commun. 270, 780-786
5. Roth, E. F., Jr., Elbaum, D., and Nagel, R. L. (1975) Blood 45, 377-386
6. Elbaum, D., Harrington, J. P., Roth, E. F., Jr., and Nagel, R. L. (1976) Biochim. Biophys. Acta 427, 57-69
7. Hirsch, R. E., Elbaum, D., Brody, S. S., and Nagel, R. L. (1980) J. Colloid Interface Sci. 78, 212-216
8. Hebbel, R. P. (1990) Semin. Hematol. 27, 51-69
9. Sheng, K., Shariff, M., and Hebbel, R. P. (1998) Blood 91, 3467-3470
10. Harrington, J. P. (1998) Comp. Biochem. Physiol. B Biochem. Mol. Biol. 119, 305-309
11. Fung, L. W. N., Lin, K. L. C., and Ho, C. (1975) Biochemistry 14, 3424-3430
12. Russu, I. M., and Ho, C. (1982) Biochemistry 21, 5044-5051
13. Fronticelli, C., and Bucci, E. (1978) in Biochemical and Clinical Aspects of Hemoglobin Abnormalities (Caughey, W. S., ed), Academic Press, NY
14. Fronticelli, C., and Gold, R. (1976) J. Biol. Chem. 251, 4968-4972
15. Fronticelli, C. (1978) J. Biol. Chem. 253, 2288-2291
16. Okonjo, K. (1980) J. Biol. Chem. 255, 3274-3277
17. Elbaum, D., Hirsch, R. E., and Nagel, R. L. (1981) in Molecular Basis of Mutant Hemoglobin Dysfunction (Sigler, P. B., ed) Vol. 1, pp. 253-258, Elsevier, NY
18. Ueda, Y., Bookchin, R. M., and Nagel, R. L. (1978) Biochem. Biophys. Res. Commun. 85, 526-531
19. Klipstein, F. A., and Ranney, H. M. (1960) J. Clin. Invest. 39, 1894-1899
20. Shaklai, N., Yguerabide, J., and Ranney, H. M. (1977) Biochemistry 16, 5585-5592
21. Shaklai, N., Sharma, V. S., and Ranney, H. M. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 65-68
22. Walder, J. A., Chatterjee, R., Steck, T. L., Low, P. S., Musso, G. F., Kaiser, E. T., Rogers, P. H., and Arnone, A. (1984) J. Biol. Chem. 259, 10238-10246
23. Ip, S. H. C., Johnson, M. L., and Ackers, G. K. (1976) Biochemistry 15, 654-660
24. Bunn, H. F. (1972) in Hemoglobin and Red Cell Structure and Function (Brewer, G. J., ed), pp. 41-53, Plenum Press, NY
25. Pennelly, R. R., and Noble, R. W. (1978) in Biochemical and Clinical Aspects of Hemoglobin Abnormalities (Caughey, W. S. ed), Academic Press, NY
26. DeYoung, A., and Noble, R. W. (1981) Methods Enzymol. 76, 792-803
27. Eaton, W. A., and Hofrichter, J. (1990) Adv. Protein Chem. 40, 63-279
28. MacQuarrie, R., and Gibson, Q. H. (1971) J. Biol. Chem. 246, 5832-5835
29. MacQuarrie, R., and Gibson, Q. H. (1972) J. Biol. Chem. 247, 5686-5694
30. Gottfried, G. S., Juszczak, L. J., Fataliev, N. A., Acharya, A. S., Hirsch, R. E., and Friedman, J. M. (1997) J. Biol. Chem. 272, 1571-1578
31. Hirsch, R. E. (1994) Methods Enzymol. 232, 231-246
32. Burstein, E. A., Vederkonra, N. S., and Ivkova, M. N. (1973) Photochem. Photobiol. 18, 263-279
33. Steiner, R. F., and Weinryb, I. (1971) Excited States of Proteins and Nucleic Acids, Plenum Press, NY
34. Lakowicz, J. R. (1983) Principles of Fluorescence Spectroscopy, Plenum Press, NY
35. Su, C., Park, Y. D., Liu, G., and Spiro, T. G. (1989) J. Am. Chem. Soc. 111, 3457-3459
36. Austin, J., Jordan, T., and Spiro, T. G. (1993) in Biomolecular Spectroscopy, Part A, (Clark, R. J. H., and Hester, R. E., eds) pp. 55-125, John Wiley & Sons, NY
37. Hu, X., and Spiro, T. G. (1997) Biochemistry 36, 15701-15712
38. Scott, T. W., Friedman, J. M., Ikeda-Saito, M., and Yonetani, T. (1983) FEBS Lett. 158, 68-72
39. Scott, T. W., Friedman, J. M., and Macdonald, V. W. (1985) J. Am. Chem. Soc. 107, 3702-3705
40. Jayaraman, V., Rodgers, K. R., Mukerji, I., and Spiro, T. G. (1995) Science 269, 1843-1848
41. Huang, S., Peterson, E., Ho., C., and Friedman, J. M. (1997) Biochemistry 36, 6197-6206
42. Rodgers, K. R., and Spiro, T. G. (1994) Science 285, 1697-1699
43. Wang, D., and Spiro, T. G. (1998) Biochemistry 37, 9940-9951
44. Huang, J., Juszczak, L. J., Peterson, E. S., Shannon, C., Yang, M., Huang, S., Vidugiris, G. V. A., and Friedman J. M. (1999) Biochemistry, in press
45. Juszczak, L. J., Hirsch, R. E., Nagel, R. L., and Friedman, J. M. (1998) J. Raman Spectrosc. 29, 963-968
46. Miura, T., Takeuchi, H., and Harada, I. (1989) J. Raman Spectrosc. 20, 667-671
47. Maruyama, T., and Takeuchi, H. (1995) J. Raman Spectrosc. 26, 319-324
48. Sokolov, L., and Mukerji, I. (1998) J. Phys. Chem. B 102, 8314-8319
49. Lin, M. J., Rao, M. J., Friedman, J. M., Acharya, A. S., and Hirsch, R. E. (1991) Biophys. J. 59, 290a
50. Hirsch, R. E., Lin, M. J., Rao, M. J., and Acharya, A. S. (1991) Blood 78, Suppl. 1, 199a
51. Hirsch, R. E., Lin, M. J., Rao, M. J., and Acharya, A. S. (1992) Biophys. J. 61, A57
52. Hirsch, R. E., Zukin, R. S., and Nagel, R. L. (1980) Biochem. Biophys. Res. Commun. 93, 432-439
53. Zentz, C., Pin, S., and Alpert, B. (1994) Methods Enzymol. 232, 247-266
54. Geraci, G., and Parkhurst, L. J. (1981) Methods Enzymol. 76, 262-275
55. Melki, G. (1971) Biochim. Biophys. Acta 263, 226-243
56. Reiss, G. H., Ranney, H. M., and Shaklai, N. (1982) J. Clin. Invest. 70, 946-952
57. Padlan, E. A., and Love, W. E. (1985) J. Biol. Chem. 260, 8272-8279
58. Padlan, E. A., and Love, W. E. (1985) J. Biol. Chem. 260, 8280-8291
59. Harrington, D. J., Adachi, K., and Royer, W. E., Jr. (1997) J. Mol. Biol. 272, 398-407