Conformational Changes Involved in the Switch from Ovalbumin to S-Ovalbumin

Zeitschrift fur Naturforschung - Section C Journal of Biosciences

Volumn 51, Issue 5, 1996, Pages 379-385

  Castellano, Agostina Congiu ^a   Bianconi, Antonio ^a   Bruni, Fabio ^a   Paolinellia, Corrado ^a   Barteri, Mario ^b   Longac, Stefano Delia ^c  

^a UNIVERSITÀ DI ROMA LA SAPIENZA   (Italy)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

^c UNIVERSITY OF L'AQUILA   (Italy)

Author keywords

Conformational Change; Denatured State; Protein Folding; Synchrotron Radiation; X Ray Scattering

Indexed keywords

OVALBUMIN;

ANIMAL; ARTICLE; CHEMISTRY; CHICKEN; DRUG STABILITY; HEAT; KINETICS; PROTEIN CONFORMATION; PROTEIN DENATURATION; RADIATION SCATTERING; X RAY DIFFRACTION;

ANIMALS; CHICKENS; DRUG STABILITY; HEAT; KINETICS; OVALBUMIN; PROTEIN CONFORMATION; PROTEIN DENATURATION; SCATTERING, RADIATION; X-RAY DIFFRACTION;

ANIMALIA; GALLUS GALLUS;

EID: 0030150658     PISSN: 09395075     EISSN: None     Source Type: Journal    
DOI: 10.1515/znc-1996-5-615     Document Type: Article

References (28)

1. Bordas J., Koch M. H. J., Clout P. N., Dorrington E., Boulin C. and Gabriel A. (1980), A synchrotron radiation camera and data acquisition system for time resolved X-ray scattering studies. J. Phvs. E: Sci. In-strum. 13, 938-944.
2. Chan H.S. and Dill K. A. (1990), Origins of structure in globular proteins. Proc. Natl. Acad. Sci. USA 87. 6388-6392.
3. Dill K. A., Alonso D.O.V. and Hutchinson. K. (1989), Thermal stability of globular proteins. Biochemistry 28. 5439-5449.
4. Depautex C. Desvignes C., Leboucher P., Lemonnier M., Dagneaux D., Benoit J. P. and Vachette P. (1987). The small angle x-ray scattering instrument D24. LURE Annual Report.
5. Donovan J. W. and Mapes C. J. (1976), A differential scanning calorimetric study of conversion of ovalbumin to S-ovalbumin in Eggs. J. Sci. Food Agric. 27. 197-204.
6. Eliezer C. J., Chiba K., Tsuruta K., Doniach S., Hodgson K. O. and Kihara H., (1993), Evidence of an associative intermediate on the myoglobin refolding pathway. Biophvs. J. 65. 912-917.
7. Glatter O. and Kratkv O. (1982). Small Angle X-ray Scattering. Academic Press. New York
8. Guinier A. and Fournet G. (1955). Small Angle Scattering of X-rays. John Wiley & Sons, Inc., New York.
9. Honevcutt J. D. and Thirumalai D. (1992). The nature of folded states of globular proteins. Biopolymers 32. 326-709.
10. Kataoka M., Hagihara Y., Mihara K. and Goto Y. (1993), Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol. 229, 591-596.
11. Kint. S. and Tomimatsu Y. (1979), Raman difference spectroscopic investigation of ovalbumin and S-oval-bumin. Biopolvmers 18. 1073-1079.
12. Hagihara Y., Aimoto S., Fink A. L. and Goto Y. (1993), Guanidine hydrochloride-induced folding of proteins. J. Mol. Biol. 231, 80-184.
13. Matsumoto T. and Chiba. J. (1990), Rheological and small-angle X-ray scattering investigations on the shape and ordered arrangement of native ovalbumin molecules in aqueous colloids. J. Chem. Soc. Faraday Trans. 86, 2877-2882.
14. Matsumoto T. and Inoue H. (1991). Effect of heat de-naturation on the structure and rheological properties of ovalbumin aqueous colloids. J. Chem. Soc. Faraday Trans. 87, 3385-3388.
15. Matsumoto T., Inoue H. and Chiba J. (1992), Microscopic surface structure of a globular molecule of ovalbumin in aqueous buffer solutions. J. Appl. Phys. 71, 1020-1025.
16. Matsumoto T. and Inoue H. (1993), Association state, overall structure, and surface roughness of native ovalbumin molecules in aqueous solutions at various ionic concentrations. J. Coll. Interface Sci. 160, 105-109.
17. Nakamura R., Hirai M. and Takemori Y. (1980), Some differences noted between the properties of ovalbumin and S-ovalbumin in native state. Agric. Biol. Chem. 44, 149-153.
18. Nakamura R., Takemori Y. and Shitamori S. (1981), Liberation of carboxyl groups on conversion of ovalbumin to S-ovalbumin. Agric. Biol. Chem. 45, 1653-1659.
19. Nakamura R. and Ishimaru M. (1981), Changes in the shape and surface hydrophobicity of ovalbumin during its transformation to S-ovalbumin. Agric. Biol. Chem. 45. 2775-2780.
20. Sail A., Shakhnovich E. and Karplus. M. (1994), How does a protein fold? Nature 369, 248-251.
21. Smith M. B. (1964). Studies on ovalbumin I. Denaturation by heat and the heterogeneity of ovalbumin. Aust. J. Biol. Sci. 17, 261-270.
22. Smith M. B. and Back J. F. (1965), Studies on ovalbumin II. The formation and properties of S-oval-bumin, a more stable form of ovalbumin. Aust. J. Biol. Sci. 18. 36-77.
23. Smith M.B. and Back J. F. (1968), Studies on ovalbumin III. Denaturation of ovalbumin and S-ovalbumin. Aust. J. Biol. Sci. 21, 39-48.
24. Smith M. B. and Back J. F. (1968), Studies on ovalbumin IV. Trypsin digestion and the cystine peptides of ovalbumin and S-ovalbumin. Aust. J. Biol. Sci. 21, 49-58.
25. Stein P. E., Leslie A. G. W., Finch J. T. and Carrell R. (1991), Crystal structure of uncleaved ovalbumin at 1.95 A resolution. J. Mol. Biol. 221, 941-959.
26. Svergun D., Barberato C., Kozin M., Volkov V., Stuhr-mann H. B. and Kock M. H. J. (1995), New methods for solution scattering data analysis and their applications to biopolvmers. Book on 5th International Conference on Biophysics and Synchrotron radiation.
27. Taborsky G. (1974), Phosphoproteins. Adv. Protein Chem. 28, 1-210.
28. Vogel H. J. and Bridger W. A. (1982). Phosphorous-31 nuclear magnetic resonance studies of the two phos-phoserine residues of hen egg white ovalbumin. Biochemistry 21. 5825-5831.