Evidence for the molten globule state of human apo-ceruloplasmin

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1297, Issue 2, 1996, Pages 119-123

  De Filippis, Vincenzo ^a   Vassiliev, Vadim B ^b   Beltramini, Mariano ^a   Fontana, Angelo ^a   Salvato, Benedetto ^a   Gaitskhoki, Vladimir S ^b  

^a UNIVERSITY OF PADOVA   (Italy)

^b INSTITUTE OF EXPERIMENTAL MEDICINE   (Russian Federation)

Author keywords

Ceruloplasmin; Circular dichroism; Fluorescence; Molten globule; Second derivative spectroscopy

Indexed keywords

APOENZYME; BINDING PROTEIN; CERULOPLASMIN;

ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE SPECTROSCOPY; HUMAN; IN VITRO STUDY; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; ULTRAVIOLET SPECTROPHOTOMETRY;

ANILINO NAPHTHALENESULFONATES; APOPROTEINS; CERULOPLASMIN; CIRCULAR DICHROISM; COPPER; HEPATOLENTICULAR DEGENERATION; HUMANS; METALLOPROTEINS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE;

EID: 0000894285     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(96)00139-2     Document Type: Article

References (38)

1. [1] Takahashi, N., Ortel, T.L. and Putnam, F.W. (1984) Proc. Natl. Acad. Sci. USA 81, 390-394.
2. [2] Zaitseva, I., Zaitsev, V., Card, G., Moshkov, K., Bax, B., Ralph, A. and Lindley, P. (1996) J. Biol. Inorg. Chem. 1, 15-23.
3. [3] Malmstrom, B.G. (1978) in New Trends in Bioinorganic Chemistry (Williams, R.J.P. and Da Silva, J.R.F., eds.), pp. 59-77, Academic Press, New York.
4. [4] Ryden, L. (1982) Proc. Natl. Acad. Sci. USA 79, 6767-6771.
5. [5] Yoshida, K., Furihata, K., Takeda, S., Nakamura, A., Yamamoto, K., Morita, H., Hiyamuta, S., Ikeda, S., Shimizu, N. and Yanagisawa, N. (1995) Nature Genet. 9, 267-273.
6. [6] Holtzman, N.A. and Gaumnitz, B.M. (1970) J. Biol. Chem. 245, 2354-2358
7. [7] Morell, A.G. and Scheinberg, I.H. (1957) Science 127, 588-590.
8. [8] Aisen, P. and Morell, A.G. (1966) J. Biol. Chem. 240, 1974-1978.
9. [9] Jackson, G.E., May, P.M. and Williams, D.R. (1978) FEBS Lett. 90, 173-177.
10. [10] Morpurgo, L., Graziani, M.T., Avigliano, L., Desideri, A. and Mondovi, B. (1981) Israel. J. Biochem. 21, 26-29.
11. [11] Herve, M., Garnier-Suillerot, A., Tosi, L. and Steinbuch, M. (1985) J. Inorg. Biochem. 25, 121-130.
12. [12] Gunnarson, P.-O., Nylen, U. and Petterson, G. (1972) Eur. J. Biochem. 27, 572-577.
13. [13] Vassiliev, V.B, Kachurin, A.M., Rocco, G.-P., Beltramini, M., Salvato, B. and Gaitskhoki, V.S. (1996) Biochemistry (Moscow) 61, 221-229.
14. [14] Kasper, C.B. and Deutsch, H.F. (1963) J. Biol. Chem. 238, 2325-2337.
15. [15] Zakharova, E.T., Vassiliev, V.B., Gorbunova, V.N. and Shavlovski, M.M. (1983) Biokhimia (Russ.) 48, 1709-1720.
16. [16] Ryden, L. (1984) in Copper Proteins and Copper Enzymes (Lontie. R., ed.), Vol. 3, pp. 37-100. CRC Press, Boca Raton, FL.
17. [17] Carrico, R.J., Deutsch, H.F., Beinert, H. and Orme-Johnson, W.H. (1969) J. Biol. Chem. 44, 4141-4146.
18. [18] Ptitsyn, O.B. (1995) Adv. Protein Chem. 47, 83-229.
19. [19] Gill, S.G. and Von Hippel, P.H. (1989) Anal. Biochem. 182, 319-326.
20. [20] Weber, G. and Young, L.B. (1964) J. Biol. Chem. 239, 1415-1423.
21. [21] Ragone, R., Colonna, G., Balestrieri, C., Servillo, L. and Irace, G. (1984) Biochemistry 23, 1871-1875.
22. [22] Brahms, S. and Brahms, J. (1980) J. Mol. Biol. 138, 149-178.
23. [23] Noyer, M. and Putnam, F.W. (1981) Biochemistry 20, 3536-3542.
24. [24] Adman, E.T. (1991) Adv. Protein Chem. 32, 145-197.
25. [25] Manning, M.C. and Woody, R.W. (1987) Biopolymers 26, 1731-1752.
26. [26] Manning, M.C. and Woody, R.W. (1989) Biochemistry 28, 8609-8613.
27. [27] Vuilleumier, S., Sancho, J., Loewenthal, R. and Fersht, A.R. (1993) Biochemistry 32, 10303-10313.
28. [28] Strickland, E.H. (1974) CRC Crit. Rev. Biochem. 3, 113-175.
29. [29] Lakowicz, J.R. (1986) in Principles of Fluorescence Spectroscopy (Lakowicz, J.R., ed.). pp. 341-381, Plenum Press, New York.
30. [30] Mach, H., Dong, Z., Middaugh, C.R. and Lewis, R.V. (1991) Arch. Biochem. Biophys. 287, 41-47.
31. [31] Stryer, L. (1965) J. Mol. Biol. 13, 482-495.
32. [32] Fink, A.L. (1995) Annu. Rev. Biophys. Biomol. Struct. 24, 495-522.
33. [33] Kuwajima, K. (1977) J. Mol. Biol. 114, 241-258.
34. [34] Miranker, A.D. and Dobson, C.M. (1996) Curr. Opin. Struct. Biol. 6, 31-42.
35. [35] Haynie, D.T. and Freire, E. (1993) Proteins Struct. Funct. Genet. 16, 115-140.
36. [36] Jennings, P.A. and Wright, P.E. (1993) Science 262, 892-896.
37. [37] Balbach, J., Forge, V., Van Nuland, N.A., Winder, S.L., Hore, P.J. and Dobson, C.M. (1995) Nature Struct. Biol. 2, 865-870.
38. [38] Sugawara, T., Kuwajima, K. and Sugai, S. (1991) Biochemistry 30, 2698-2706.