Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 72, 2008 - Issue 8
Journal homepage
246
Views
10
CrossRef citations to date
0
Altmetric
Original Articles

Structural and Physicochemical Characteristics of Novel Basic Proteins Isolated from Duck Egg White

Supaporn NAKNUKOOLDepartment of Applied Biological Science, Faculty of Agriculture, Kagawa University
,
Shigeru HAYAKAWADepartment of Applied Biological Science, Faculty of Agriculture, Kagawa University
,
Yuanxia SUNDepartment of Applied Biological Science, Faculty of Agriculture, Kagawa University
&
Masahiro OGAWADepartment of Applied Biological Science, Faculty of Agriculture, Kagawa University
Pages 2082-2091 | Received 18 Mar 2008, Accepted 30 Apr 2008, Published online: 22 May 2014

  • 1) Burley, R. W., and Vadehra, D. V., The albumen: chemistry. In “The Avian Egg: Chemistry and Biology,” Wiley-Interscience, New York, pp. 65–128 (1989).
  • 2) Li-Chan, E. C. Y., Powrie, W. D., and Nakai, S., The chemistry of eggs and egg products. In “Egg Science and Technology” 4th edited, eds. Stadelman, W. J., and Cotterill, O. J., The Haworth Press, New York, pp. 105–175 (1995).
  • 3) Kovacs-Nolan, J., Phillips, M., and Mine, Y., Advances in the value of eggs and egg components for human health. J. Agric. Food Chem., 53, 8421–8431 (2005).
  • 4) Mine, Y., Egg proteins and peptide in human health: chemistry, bioactivity and production. Curr. Pharm. Des., 13, 875–884 (2007).
  • 5) Gilbert, A. B., The egg: its physical and chemical aspects. In “Physiology and Biochemistry of the Domestic Fowl” Vol. 3, eds. Bell, D. J., and Freeman, B. M., Academic, New York, pp. 1379–1399 (1971).
  • 6) Vadehra, D. V., and Nath, K. R., Eggs as a source of protein. CRC Crit. Rev. Food Technol., 4, 193–309 (1973).
  • 7) Awade, A. C., and Efstathiou, T., Comparison of three liquid chromotographic methods for egg white protein analysis. J. Chromatogr. B Biomed. Sci. Appl., 723, 69–74 (1999).
  • 8) Desert, C., Dubiard-Guerin, C., Nau, F., Jan, G., Val, F., and Mallard, J., Comparison of different electrophoretic separations of hen egg white proteins. J. Agric. Food Chem., 49, 4553–4561 (2001).
  • 9) Raikos, V., Hansen, R., Campbell, L., and Euston, S. R., Separation and identification of hen egg protein isoform using SDS–PAGE and 2D gel electrophoresis with MALDI-TOF mass spectrometry. Food Chem., 99, 702–710 (2006).
  • 10) Guerin-Dubiard, C., Pasco, M., Molle, D., Desert, T., Croguennec, T., and Nau, F., Proteomic analysis of hen egg white. J. Agric. Food Chem., 54, 3901–3910 (2006).
  • 11) Simpson, R. J., and Morgan, F. J., Isolation and complete amino acid sequence of a basic low molecular weight protein from black swan egg white. Int. J. Pept. Prot. Res., 22, 476–481 (1983).
  • 12) Odani, S., Koide, T., Ono, T., Takahashi, Y., and Suzuki, J., Covalent structure of a low-molecular-mass-protein, meleagrin, present in a turkey (Meleagris gallopavo) ovomucoid preparation. J. Biochem., 105, 660–663 (1989).
  • 13) Prager, E. M., and Wilson, A. C., Multiple lysozyme of duck egg white. J. Biol. Chem., 246, 523–530 (1971).
  • 14) Herman, J., Jolles, J., and Jolles, P., The disulfide bridges of duck egg-white lysozyme II. Arch. Biochem. Biophys., 158, 355–358 (1973).
  • 15) Kondo, K., Fujio, H., and Amano, T., Chemical and immunological properties and amino acid sequences of three lysozyme from Peking-duck egg white. J. Biochem., 91, 571–587 (1982).
  • 16) Warwas, M., Gburek, J., Osada, J., and Golab, K., Purification and characterization of cystatin from duck egg white. Acta Biochim. Polonica, 42, 351–356 (1995).
  • 17) Nagase, H., Edward, D., Harris Jr., E. D., and Brew, K., Evidence for a thio ester in duck ovostatin (ovomacroglobulin). J. Biol. Chem., 261, 1421–1426 (1986).
  • 18) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685 (1970).
  • 19) Gish, W., WU-Blast2 (Washington University Basic Local Alignment Search Tool Version 2.0), Department of Genetics, Washington University, St. Louis, http://www.ebi.ac.uk/blast2/index.html (2006).
  • 20) Thompson, J. D., Higgins, D. G., and Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673–4680 (1994).
  • 21) Saitou, N., and Nei, M., The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol., 4, 406–425 (1987).
  • 22) Felsenstein, J., Confidence limits on phylogenies: an approach using the bootstrap. Evolution, 39, 783–791 (1985).
  • 23) Beverridge, T., Toma, S. J., and Nakai, S., Determination of SH- and SS-groups in some food proteins using Ellman’s reagent. J. Food Sci., 39, 49–51 (1974).
  • 24) Sibley, C. G., and Monroe, B. L., “Distribution and Taxonomy of Birds of the World,” Yale University Press, New Haven, pp. 11–33 (1990).
  • 25) Suzuki, N., Laskowski, M., and Lee, Y. C., Phylogenetic expression of Galα1-4Gal on avian glycoproteins: glycan differentiation inscribed in the early history of modern birds. Proc. Natl. Acad. Sci. USA, 101, 9023–9028 (2004).
  • 26) Ciuraszkiewicz, J., Olczak, M., and Watorek, W., Isolation, cloning and sequencing of transferrins from red-eared turtle, African ostrich, and turkey. Comp. Biochem. Physiol. B, 144, 301–310 (2006).
  • 27) Sun, Y., and Hayakawa, S., Sequential comparison of peptides containing half cysteine residues from ovalbumins of six avian species. Biosci. Biotechnol. Biochem., 65, 2589–2596 (2001).
  • 28) Campbell, L., Raikos, V., and Euston, S. R., Modification of functional properties of egg-white proteins. Nahrung, 6, 369–376 (2003).
  • 29) Mine, Y., Noutomi, T., and Haga, N., Thermally induced changes in egg white proteins. J. Agric. Food Chem., 38, 2122–2125 (1990).
  • 30) Mine, Y., Recent advances in the understanding of egg white protein functionality. Trends Food Sci. Tech., 6, 225–232 (1995).
  • 31) Donovan, J. W., and Ross, K. D., Nonequivalence of the metal binding sites of conalbumin: calorimetric and spectrophotometric studies of aluminum binding. J. Biol. Chem., 250, 6022–6025 (1975).
  • 32) De Man, J. M., Proteins. In “Principles of Food Chemistry,” AVI, Westport, pp. 86–134 (1979).
  • 33) Zscherp, C., Aygun, H., Engels, J. M., and Mantele, W., Effect of proline to alanine mutation on the thermal stability of the all-β-sheet protein tendamistat. Biochim. Biophys. Acta, 1651, 139–145 (2003).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.