Subunit distribution of calcium-binding sites in Lumbricus terrestris hemoglobin

Journal of Protein Chemistry

Volumn 19, Issue 2, 2000, Pages 139-149

  Kuchumov, Askar R ^a   Loo, Joseph A ^b   Vinogradov, Serge N ^a  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b PFIZER INC   (United States)

Author keywords

Calcium content; Calcium binding sites; Hemoglobin; Lumbricus terrestris

Indexed keywords

CALCIUM ION; COPPER; CYSTEINE; HEMOGLOBIN; SUPEROXIDE DISMUTASE; ZINC;

ANNELID WORM; ARTICLE; BINDING SITE; CALCIUM BINDING; DISULFIDE BOND; HEMOGLOBIN ANALYSIS; NONHUMAN; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN ISOLATION; PROTEIN LOCALIZATION;

ANIMALS; BINDING SITES; CALCIUM; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; COPPER; EDETIC ACID; ENZYME STABILITY; HEMOGLOBINS; MODELS, MOLECULAR; MOLECULAR WEIGHT; OLIGOCHAETA; OXIDATION-REDUCTION; OXYGEN; PROTEIN CONFORMATION; PROTEIN SUBUNITS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROMETRY, X-RAY EMISSION; ZINC;

ANNELIDA; LUMBRICUS; LUMBRICUS TERRESTRIS;

EID: 0033914362     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1007086717412     Document Type: Article

References (55)

1. Antonini, A., and Chiancone, E. (1977). Annu. Rev. Biophys. Bioeng. 6, 239-271.
2. Blacklow, S., and Kim, P. S. (1996). Nature Struct. Biol. 3, 758-761.
3. Chiancone, E., Bull, T. E., Norne, J. E., Forsen, S., and Antonini, E. (1976). J. Mol. Biol. 107, 25-34.
4. Chiancone, E., Ferruzzi, G., Bonaventura, C., and Bonaventura, J. (1980). Biochim. Biophys. Acta 670, 84-92.
5. Chottard, G., El Ajouz, N., and Hervé, G (1992). Biochim. Biophys. Acta 1122, 113-117.
6. Chung, M. C. C., and Ellerton, H. D. (1979). Progr. Biophys. Mol. Biol. 35, 51-102.
7. De Haas, F., Taveau, J.-C., Boisset, N., Lambert, O., Vinogradov, S. N., and Lamy, J. N. (1996a). J. Mol. Biol. 255, 140-163.
8. De Haas, F., Taveau, J.-C., Boisset, N., Lambert, O., Vinogradov, S. N., and Lamy, J. N. (1996b). Biophys. J. 70, 1973-1984.
9. De Haas, F., Zal, F., Lallier, F. H., Toulmond, A., and Lamy, J. N. (1996c). Proteins Struct. Funct. Genet. 26, 241-256.
10. De Haas, F., Zal, F., You, V., Lallier, F., Toulmond, A., and Lamy, J. N. (1996d). J. Mol. Biol. 264, 111-120.
11. De Haas, F., Kuchumov, A., Taveau, J.-C., Boisset, N., Vinogradov, S. N., and Lamy, J. N. (1997). Biochemistry 36, 7330-7338.
12. Fass, D., Blacklow, S., Kim, P. S., and Berger, J. M. (1997). Nature 388, 691-693.
13. Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., and Whitehouse, C. M. (1980). Science 246, 64-71.
14. Fushitani, K., Higashiyama, K., Asao, M., and Hosokawa, K. (1996). Biochim. Biophys. Acta 1292, 273-280.
15. Gotoh, T., and Suzuki, T. (1990). Zool. Sci. 7, 1-16.
16. Green, B. G., Bordoli, R. S., Hanin, L. G., Lallier, F. H., Toulmond, A., and Vinogradov, S. N. (1999). J. Biol. Chem. 274, 28206-2812.
17. Harrington, J. P. (1994). Comp. Biochem. Physiol. 109A, 799-802.
18. Krebs, A., Kuchumov, A. R., Shaarma, P. K., Braswell, E. H., Zipper, P., Weber, R. E., Chottard, G., and Vinogradov, S. N. (1996). J. Biol. Chem. 271, 18695-18704.
19. Kuchumov, A. R., Taveau, J.-C., Lamy, J. N., Wall, J. S., Weber, R. E. and Vinogradov, S. N. (1999). J. Mol. Biol. 289, 1361-1374.
20. Lamy, J. N., Green, B. N., Toulmond, A., Walls, J. S., Weber, R. E., and Vinogradov, S. N. (1996). Chem. Rev. 96, 3113-3124.
21. Liochev, S. I., Kuchumov, A. R., Vinogradov, S. N., and Fridovich, I. (1996). Arch. Biochem. Biophys. 330, 281-284.
22. Loo, J. A., and Pesch, R. (1994). Anal. Chem. 66, 3659-3663.
23. Loo, J. A., Edmunds, C. G., and Smith, R. D. (1993). Anal. Chem. 65, 4225-4238.
24. Mainwaring, M. G., Lugo, S. D., Fingal, R. A., Kapp, O. H., and Vinogradov, S. N. (1986). J. Biol Chem. 261, 10899-10908.
25. Martin, P. D., Eisele, K. L., Doyle, M. A., Kuchumov, A. R., Walz, D. A., Arutyunyan, E. G., Vinogradov, S. N., and Edwards, B. F. P. (1996). J. Mol. Biol. 255, 170-175.
26. Ochiai, T. (1984). Arch. Biochem. Biophys. 231, 136-143.
27. Ochiai, T., Hoshina, S., and Usuki, I. (1993). Biochim. Biophys. Acta 1203, 310-314.
28. Ownby, D. W., Zhu, H., Schneider, K., Beavis, R. C., Chait, B. T., and Riggs, A. F. (1993). J. Biol. Chem. 268, 13539-13547.
29. Perutz, M. (1990). Mechanisms of Cooperativity and Allosteric Regulation in Proteins, Cambridge University Press, Cambridge.
30. Polidori, G., Maionwaring, M. G., Kosinski, T., Schwarz, C., Fingal, R. A., and Vinogradov, S. N. (1984). Arch. Biochem. Biophys. 233, 800-814.
31. Polidori, G., Mainwaring, M. G., and Vinogradov, S. N. (1988). Comp. Biochem. Physiol. 89A, 541-545.
32. Rokosz, M. J., and Vinogradov, S. N. (1982). Biochim. Biophys. Acta 707, 291-293.
33. Royer, W. E., Jr., Pardanani, A., Gibson, Q. E., Peterson, E. S., and Friedman, J. M. (1996). Proc. Natl. Acad. Sci. USA 93, 14526-14531.
34. Schatz, M., Orlova, E. V., Dube, P., Jäger, J., and Van Heel, M. (1995). J. Struct. Biol. 114, 28-40.
35. Senko, M. W., and McLafferty, F. W. (1994). Annu. Rev. Biophys. Biomol. Struct. 23, 763-785.
36. Sharma, P. K., Kuchumov, A., Chottard, G., Martin, P. D., Wall, J. S., and Vinogradov, S. N. (1996). J. Biol. Chem. 271, 8754-8762.
37. Smith, R. M., and Martell, A. E. (1989). Critical Stability Constants, Vol. 6, Plenum Press, New York, p. 96.
38. Standley, P. M., Mainwaring, M. G., Gotoh, T., and Vinogradov, S. N. (1988). Biochem. J. 249, 915-916.
39. Suzuki, T., and Riggs, A. F. (1993). J. Biol. Chem. 268, 1354-1361.
40. Suzuki, T., Takagi, T., and Ohta, S. (1990a). J. Biol. Chem. 265, 1551-1555.
41. Suzuki, T., Takagi, T., and Gotoh, T. (1990b). J. Biol. Chem. 265, 12168-12177.
42. Suzuki, T., Ohta, T., Yasa, H. J., and Takagi, T. (1994). Biochim. Biophys. Acta 1217, 291-296.
43. Taveau, J.-C., Boisset, N, Vinogradov, S. N., and Lamy, J. N. (1999). J. Mol. Biol. 289, 1343-1349.
44. Tsuneshige, A., Imai, K., Hori, H., Tyuma, I., and Gotoh, T. (1989). J. Biochem. 106, 406-417.
45. Vinogradov, S. N., Shlom, J. M., Hall, B. C., Kapp, O. H., and Mizukami, H. (1977). Biochim. Biophys. Acta 492, 136-155.
46. Vinogradov, S. N. (1985). In Respiratory Pigments in Animals (Lamy, J., Truchot, J. P., and Gilles, R., eds.), Springer-Verlag, Berlin. pp. 9-20.
47. Vinogradov, S. N., and Sharma, P. K. (1994). Meth. Enzmol. 231, 112-124.
48. Vinogradov, S. N., Kapp, O. H., and Ohtsuki, M. (1982). Electron Microscopy of Proteins, Vol. 3 (Harris, J., ed.), Academic Press, New York. p. 135.
49. Vinogradov, S. N., Standley, P. R., Mainwaring, M. G., Kapp, O. H., and Crewe, A. V. (1985). Biochim. Biophys. Acta 828, 43-50.
50. Vinogradov, S. N., Lugo, S. D., Mainwaring, M. G., Kapp, O. H., and Crewe, A. V. (1986). Proc. Natl. Acad. Sci. USA 83, 8034-8038.
51. Vinogradov, S. N., Sharma, P. K., Qabar, A. N., Wall, J. S., Westrick, J. A., Simmons, J. H., and Gill, S. J. (1991). J. Biol. Chem. 266, 13091-13096.
52. Vinogradov, S. N., Walz, D. A., Pohajdak, B., Moens, L., Kapp, O. H., Suzuki, T., and Trotman, C. N. A. (1993). Comp. Biochem. Physiol. 106B, 1-26.
53. Weber, R. E., and Vinogradov, S. N. (2000). Physiol. Rev. (in press).
54. Zhu, H., Hargrove, M., Xie, Q., Nozaki, Y., Linse, K., Smith, S. S., Olson, J. S., and Riggs, A. F. (1996a). J. Biol. Chem. 271, 29999-30006.
55. Zhu, H., Ownby, D. W., Riggs, C. K., Nolasco, N. J., Stoops, J. K., and Riggs, A. F. (1996b). J. Biol. Chem. 271, 30007-30021.