Ovalbumin

Catalog Number

O8075

Form

Supplied as a purified lyophilized powder. No preservatives added. Reconstitute in distilled water or a dilute buffer to required concentration.

References

US Biological application reference: Swearingen, K.E. et al., (2008) J. Chromatography A 1194: 249-252. \n\nAhmad, F., and Salahuddin, A.: The Denatured State of Ovalbumin, Biochem. J., 128, 49P (1972).\n\nAmbrosino, R., Barone, G., Castronuovo, G., Ceccarini, C., Cultrera, O., and Elia, V.: Protein-Ligand Interaction. A Calorimetric Study of the Interaction\nof Oliogsaccharides and Hen Ovalbumin Glycopeptides with Concanavalin A, Biochem., 26, 3971 (1987).\n\nAnsari, A., Ahmad, R., and Salahuddin, A.: The Native and Denatured States of Ovalbumin, Biochem. J., 126, 447 (1972).\n\nAnsari, A., Kidwai, S., and Salahuddin, A.: Acetylation of Amino Groups and Its Effect on the Conformation and Immunological Activity of Ovalbumin,\nJ. Biol. Chem., 250, 1625 (1975).\n\nBatra, P.: Conformational Stability of Citraconylated Ovalbumin, Intl. J. Biochem., 23, 1375 (1991).\n\nCaslavska, J., Gebauer, P., and Thormann, W.: Purification of Ovalbumin and Lysozyme from a Commercial Product by Recycling Isotachophoresis, J.\nChromatography, 585, 145 (1991).\n\nConchie, J., Hay, A., Strachan, I., and Levvy, G.: The Enzymatic Degradation of Ovalbumin and Its Glycopeptides, Biochem. J., 115, 717 (1969).\n\nCunningham, L., Ford, J., and Rainey, J.: Heterogeneity of [[beta]]-Aspartyl-Oligosaccharides Derived from Ovalbumin, Biochim. Biophys. Acta, 101,\n233 (1965).\n\nFothergill, L., and Fothergill, J.: Disulphide Bonds of Ovalbumins, Biochem. J., 110, 36P (1968).\n\nFothergill, L., and Fothergill, J.: Structural Comparison of Ovalbumin from Nine Different Species, Eur. J. Biochem., 17, 529 (1970).\n\nFothergill, L., and Fothergill, J.: Thiol and Disulphide Contents of Hen Ovalbumin. C-Terminal Sequence and Location of Disulphide Bond, Biochem. J.,\n116, 555 (1970).\n\nFranklin, J., and Leslie, J.: The Kinetics of the Reaction of N-Ethylmaleimide with Denatured [[beta]]-Lactoglobulin and Ovalbumin, Biochim. Biophys.\nActa, 160, 333 (1968).\n\nGilbert, G., and Kellett, G.: Interacting Systems of the Type A + B -> <- C Ovalbumin and Myoglobulin, J. Biol. Chem., 246, 6079 (1971).\n\nGilmore, L., and Fothergill, J.: The Thiol and Disulphide Contents of Immunologically Related Ovalbumins, Biochem. J., 103, 39P (1967).\n\nGlabe, C., Hanover, J., and Lennarz, W.: Glycosylation of Ovalbumin Nascent Chains, J. Biol. Chem., 255, 9236 (1980).\n\nGorbunoff, M.: Exposure of Tyrosine Residues in Protein. III. The Reaction of Cyanuric Fluoride in N-Acetylimidazol with Ovalbumin, Chymotrypsin and\nTrypsinogen, Biochem., 8, 2591 (1969).\n\nGoux, W., and Venkatasubramanian, P.: Metal Ion Binding Properties of Hen Ovalbumin and S-Ovalbumin: Characterization of the Metal Ion Binding Site\nby 31P NMR and Water Proton Relaxation Rate Enhancements, Biochem., 25, 84 (1986).\n\nHolt, J., and Greeth, J.: Studies of the Denaturation and Partial Renaturation of Ovalbumin, Biochem. J., 129, 665 (1972).\n\nHowlett, G., and Nichol, L.: A Sedimentation Equilibrium Study of the Interaction between Ovalbumin and Lysozyme, J. Biol. Chem., 248, 619 (1973).\n\nHuang, C., and Montgomery, R.: Enzymatic Degradation of the Components of Asparaginyl-Carbohydrate from Chicken Ovalbumin, Biochem. Biophys.\nRes. Comm., 37, 94 (1969).\n\nKato, Y., Iwase, H., and Hota, K.: Characterization of a Highly Glycosylated Biosynthetic Intermediate of Ovalbumin, Arch. Biochem. Biophys., 244, 408\n(1986).\n\nKato, Y., Iwase, H., and Hotta, K.: Comparative Study of Chicken Ovalbumin Subfractions Having Different Carbohydrate Chain from Each Other by High\nPerformance Anion Exchange Chromatography, Comp. Biochem. Physiol., Pt. B., 90, 37 (1988).\n\nKatz, S., and Miller, J.: Structure-Volume Relationships for Proteins, Comparative Dilatometric Study of Acid-Base Reactions of Lysozyme and\nOvalbumin in Water and Denaturing Media, Biochem., 10, 3569 (1971).\n\nKitabatake, N., Indo, K., and Doi, E.: Limited Proteolysis of Ovalbumin by Pepsin, J. Agr. Food Chem., 36, 417 (1988).\n\nKitabatake, N., Indo, K., and Doi, E.: Changes in Interfacial Properties of Hen Egg Ovalbumin Caused by Freeze-Drying and Spray-Drying, J. Agr. Food\nChem., 37, 905 (1989).\n\nKoseki, T., Kitabatake, N., and Doi, E.: Freezing Denaturation of Ovalbumin at Acid pH, J. Biochem. Japan, 107, 389 (1990).\n\nLevison, P., Badger, S., Toome, D., Koscielny, M., Lane, L., and Butts, E.: Economic Considerations Important in the Scale-Up of an Ovalbumin Separation\nfrom Hen Egg-White on the Anion-Exchange Cellulose DE92, J. Chromatography, 590, 49 (1992).\n\nLinderstrom -Lang, K., and Otteseen, M.: A New Protein from Ovalbumin, Nature, 159, 807 (1947).\n\nLiss, M., and Edelstein, L.: Evidence for the Enzymatic Methylation of Crystalline Ovalbumin Preparations, Biochem. Biophys. Res. Comm., 26, 497\n(1967).\n\nMakino, M., and Yamashina, I.: Periodate Oxidation of Glycopeptides from Ovalbumin, J. Biochem. Japan, 60, 262 (1966).\n\nMarcinkiewica, J. Chain, B., Olszowska, E., Olszowski, S., and Zgliczynski, J.: Enhancement of Immunogenic Properties of Ovalbumin as a Result of Its\nChlorination, Intl. J. Biochem., 23, 1393 (1991).\n\nMatsudomi, N., Ishimura, Y., and Kato, A.: Improvement of Gelling Properties of Ovalbumin by Heating in Dry State, Agr. Biol. Chem., Tokyo, 55, 879\n(1991).\n\nMilstein, C.: An Application of Diagonal Electrophoresis to the Selective Purification of Serine Phosphate Peptides. Serine Phosphate Peptides from\nOvalbumin, Biochem. J., 110, 127 (1968).\n\nMine, Y., Noutomi, T., and Haga, N.: Emulsifying and Structural Properties of Ovalbumin, J. Agr. Food Chem., 39, 443 (1991).\n\nMontgomery, R., Lee, Y., and Wu, Y.: Glycopeptides from Ovalbumin. Preparation, Properties, and Partial Hydrolysis of the Asparaginyl Carbohydrate,\nBiochem., 4, 566 (1965).\n\nNakai, S., and Kason, C.: A Fluorescence Study of the Interactions Between [[kappa]] and [[alpha]] s1-Casein and Between Lysozyme and Ovalbumin,\nBiochim. Biophys. Acta, 351, 21 (1974).\n\nNarita, K., and Ishii, J.: N-Terminal Sequence in Ovalbumin, J. Biochem. Japan, 52, 367 (1962).\n\nNichol, L., Owen, E., and Winzor, D.: A Macromolecular Shape Function Based on Sedimentation Velocity Parameters, Arch. Biochem. Biophys., 236, 338\n(1985).\n\nNiu, C., and Fraenkel-Conrat, H.: Determination of C-Terminal Amino Acids and Peptides by Hydrazinalysis, J. Am. Chem. Soc., 77, 5882 (1955).\n\nOttesen, M., and Wallevik, K.: Use of the pH-Stat for Measuring the Denaturation of Ovalbumin in Acid Solutions, Biochim. Biophys. Acta, 160, 262\n(1968).\n\nPerlmann, G.: Enzymatic Dephosphorylaton of Ovalbumin and Plakalbumin, J. Gen. Physiol, 35, 711 (1952).\n\nSchweers, L., Frank, D., Weigel, N., and Sanders, M.: The Steroid-Dependent Regulatory Element in the Ovalbumin Gene Does Not Function as a Typical\nSteroid Response Element, J. Biol. Chem., 265, 7590 (1990).\n\nStein, P., Leslie, A., Finch, J., Turnell, W., Mclaughlin, P., and Carrell, R.: Crystal Structure of Ovalbumin as a Model for the Reactive Centre of Serpins,\nNature, 347, 99 (1990).\n\nStein, P., Leslie, A., Finch, J., and Carrell, R.: Crystal Structure of Uncleaved Ovalbumin at 1.95