Abstract
Penalbumin (PEN), a newly discovered sulfhydryl-containing glycoprotein from egg whites of penguins(Sphenisciformes), is a major constituent of all penguin egg whites studied, but it is low or very low in most other egg whites studied. Adelie penguin(Pygoscelis adeliae) egg white contains ∼30% ovalbumin (POVAL) and 25% PEN, while chicken egg white contains ∼55% ovalbumin (COVAL) and <0.01% PEN. PEN has a molecular weight of 61,000 and contains 15% carbohydrate and two sulfhydryl groups, but no phosphates. POVAL has a molecular weight of 48,000 and contains 7% carbohydrate, three sulfhydryl groups, and one phosphate. Penguin serum albumin (PSA) has properties which are very similar to bovine serum albumin (BSA), and the composition and properties of PEN were suggestive of an ancestral relationship to POVAL and COVAL. PEN reacts slowly with 5,5′-dithiobis(2-nitrobenzoic acid) (DTNB), while POVAL reacts rapidly. On simultaneous addition of DTNB and cystamine (β,β′-diaminodiethyl disulfide) the rate of reaction with PEN was increased, but not with POVAL.
Similar content being viewed by others
References
Allen, R. J. L. (1940).Biochem. J. 34, 858–865.
Allison, R. G., and Feeney, R. E. (1968).Arch. Biochem. Biophys. 124, 548–555.
Atkinson, P. H., Grey, A., Carver, J. P., Hakimi, J., and Ceccarini, C. (1981).Biochemistry 20, 3979–3986.
Baker, C. M. A., and Manwell, C. (1975). In Stonehouse, B. (ed.),The Biology of Penguins, University Park Press, Baltimore, Maryland, pp. 43–56.
Castrelos, O. D., Mercado, M. R., Abatángelo, C., and Margni, R. A. (1975).Biochim. Biophys. Acta 400, 137–142.
Chervenka, C. H. (1969).A Manual of Methods for the Analytical Ultracentrifuge, Beckman Instruments, Palo Alto, California.
Clark, J. R., Osuga, D. T., and Feeney, R. E. (1963).J. Biol. Chem. 238, 3621–3631.
Cohn, E. J., and Edsall, J. T. (1965). In Cohn, E. J., and Edsall, J. T. (eds.),Proteins, Amino Acids, and Peptides as Ions and Dipolar Ions, Hefner, New York, pp. 370–381.
Davis, B. J. (1964).Ann. NY Acad. Sci. 121, 404–427.
Dubois, M., Giles, K. A., Hamilton, J. K., Rebers, P. A., and Smith, F. (1956).Anal. Chem. 28, 350–356.
Edelhock, H. (1967).Biochemistry 6, 1948–1954.
Elson, L. A., and Morgan, W. T. J. (1933).Biochem. J. 27, 1824–1828.
Feeney, R. E. (1982).Int. J. Peptide Protein Res. 19, 215–232.
Feeney, R. E., and Allison, R. G. (1969).Evolutionary Biochemistry of Proteins: Homologous and Analogous Proteins from Avian Egg Whites, Blood Sera, Milk, and Other Substances, Wiley, New York.
Feeney, R. E., and Komatsu, S. K. (1966).Struct. Bonding 1, 149–206.
Feeney, R. E., and Osuga, D. T. (1976).Comp. Biochem. Physiol. 54A, 281–286.
Feeney, R. E., Rhodes, M. B., and Anderson, J. S. (1960).J. Biol. Chem. 235, 2633–2637.
Feeney, R. E., Osuga, D. T., Lind, S. B., and Miller, H. T. (1966).Comp. Biochem. Physiol. 18, 121–130.
Feeney, R. E., Allison, R. G., Osuga, D. T., Bigler, J. C., and Miller, H. T. (1968).Antarctic Res. Series 12, 151–165.
Fernandez Diez, M. J., Osuga, D. T., and Feeney, R. E. (1964).Arch. Biochem. Biophys. 107, 449–458.
Fothergill, L. A., and Fothergill, J. E. (1970).Biochem. J. 116, 555–561.
Gibbons, R. A. (1972). In Gottschalk, A. (ed.),Glycoproteins. Their Composition, Structure and Function, Part A, Elsevier, New York, pp. 31–140.
Grassetti, D. R., and Murray, J. F., Jr. (1967).Arch. Biochem. Biophys. 119, 41–49.
Gray, W. R. (1972). InMethods in Enzymology, Vol. 25, pp. 121–138.
Hallaway, B. E., Hedlund, B. E., and Benson, E. S. (1980).Arch. Biochem. Biophys. 203, 332–342.
Hedrick, J. L., and Smith, A. J. (1968).Arch. Biochem. Biophys. 126, 155–164.
Hirs, C. H. W. (1967). InMethods in Enzymology, Vol. 11, pp. 197–199.
Ho, C. Y.-K., Prager, E. M., Wilson, A. C., Osuga, D. T., and Feeney, R. E. (1976).J. Mol. Evol. 8, 271–282.
Ishihara, H., Takahashi, N., Ito, J., Takeuchi, E., and Tejima, S. (1981).Biochim. Biophys. Acta 669, 216–221.
Iwase, H., Kato, Y., and Hotta, K. (1981).J. Biol. Chem. 256, 5638–5642.
Janatova, J., Crandall, R. E., and Andrade, J. D. (1980).Prep. Biochem. 10, 405–430.
Kato, I., Kohr, W. J., and Laskowski, M., Jr. (1978). In Magnusson, S., Ottesen, M., Foltmann, B., Danø, K., and Neurath, H., (eds.),Regulatory Proteolytic Enzymes and Their Inhibitors, Pergamon, New York, pp. 197–206.
Levvy, G. A., and McAllen, A. (1959).Biochem. J. 73, 127–132.
Lin, T. S., and Kolattukudy, P. E. (1980).Eur. J. Biochem. 106, 341–351.
Linderstrom-Lang, K., and Ottesen, M. (1947).Nature 159, 807–808.
Liu, W. H., Means, G. E., and Feeney, R. E. (1971).Biochim. Biophys. Acta 229, 176–185.
Malthouse, J. P. G., and Brocklehurst, K. (1980).Biochem. J. 185, 217–222.
Manwell, C., and Baker, C. M. A. (1973).Ibis 115, 586–589.
Maurer, H. R. (1971).Disc Gel Electrophoresis and Related Techniques of Polyacrylamide Gel, Walter de Gruyter, Berlin.
Means, G. E., and Feeney, R. E. (1971).Chemical Modification of Proteins, Holden-Day, San Francisco.
Means, G. E., Ryan, D. S., and Feeney, R. E. (1974).Acc. Chem. Res. 7, 315–320.
Miller H. T., and Feeney, R. E. (1966).Biochemistry 5, 952–958.
Moore, S., and Stein, W. H. (1963). InMethods in Enzymology, Vol. 6, pp. 819–831.
Nakamura, R., Takemori, Y., and Shitamori, S. (1981).Agric. Biol. Chem. 45, 1653–1659.
Narita, K. (1970). In Needleman, S. B. (ed.),Protein Sequence Determination, Springer-Verlag, New York, pp. 25–90.
Nisbet, A. D., Saundry, R. H., Moir, A. J. G., Fothergill, L. A., and Fothergill, J. E. (1981).Eur. J. Biochem. 115, 335–345.
Osuga, D. T., and Feeney, R. E. (1977). In Whitaker, J. R., and Tannenbaum, S. R. (eds.),Food Proteins, Avi, Westport, Connecticut, pp. 209–266.
Osuga, D. T., Bigler, J. C., Uy, R. L., Sjoberg, L., and Feeney, R. E. (1974).Comp. Biochem. Biophys. 48B, 519–533.
Perlmann, G. E. (1952).J. Gen. Physiol. 35, 711–726.
Peters, T., Jr. (1975). In Putnam, F. W. (ed.),The Plasma Proteins, 2nd ed., Academic, New York, Vol. 1, pp. 133–180.
Peters, T., Jr. (1980).Albumin, An Overview and Bibliography, Miles Laboratories, Elkhart, Indiana.
Prager, E. M., Wilson, A. C., Osuga, D. T., and Feeney, R. E. (1976).J. Mol. Evol. 8, 283–294.
Rhodes, M. B., Bennett, N., and Feeney, R. E. (1960).J. Biol. Chem. 235, 1686–1693.
Schachman, H. K. (1957). InMethods in Enzymology, Vol.4, pp. 32–103.
Smith, G. M., and Pettigrew, G. W. (1980).Eur. J. Biochem. 110, 123–130.
Smith, M. B. (1964).Aust. J. Biol. Sci. 17, 261–270.
Smith, M. B., and Back, J. F. (1965).Aust. J. Biol. Sci. 18, 365–377.
Smith, M. B., and Back, J. F. (1968).Aust. J. Biol. Sci. 21, 549–558.
Taborsky, G. (1974).Adv. Protein Chem. 28, 1–210.
Warren, L. (1959).J. Biol. Chem. 234, 1971–1975.
Weber, K., and Osborn, M. (1975). In Neurath, H., and Hill, R. L., (eds.),The Proteins, 3rd ed., Academic, New York, Vol. 1, pp. 197–223.
Wilson, J. M., Wu, D., Motiu-DeGrood, R., and Hupe, D. J. (1980).J. Am. Chem. Soc. 102, 359–363.
Wiseman, R. L., Fothergill, J. E., and Fothergill, L. A. (1972).Biochem. J. 127, 775–780.
Yamasaki, R. B., Shimer, D. A., and Feeney, R. E. (1981).Anal. Biochem. 111, 220–226.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Osuga, D.T., Aminlari, M., Ho, C.Y.K. et al. Sulfhydryl proteins of penguin egg white: Ovalbumin and penalbumin. Comparisons with penguin serum albumin, chicken ovalbumin, and bovine serum albumin. J Protein Chem 2, 43–62 (1983). https://doi.org/10.1007/BF01025167
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF01025167