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  • 1
    Electronic Resource
    Electronic Resource
    Protein—Protein Interactions in Aqueous Ammonium Sulfate Solutions. Lysozyme and Bovine Serum Albumin (BSA) (2000)
    Springer
    Journal of solution chemistry 29 (2000), S. 699-718 
    Details
    ISSN: 1572-8927
    Keywords: Potential of mean force ; proteins ; salts ; intermolecular interactions ; precipitation ; crystallization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Osmotic pressures have been measured to determine lysozyme—lysozyme,BSA—BSA, and lysosyme—BSA interactions for protein concentrations to 100 g-L−1in an aqueous solution of ammonium sulfate at ambient temperature, as a functionof ionic strength and pH. Osmotic second virial coefficients for lysozyme, forBSA, and for a mixture of BSA and lysozyme were calculated from theosmotic-pressure data for protein concentrations to 40 g-L−1. The osmotic second virialcoefficient of lysozyme is slightly negative and becomes more negative withrising ionic strength and pH. The osmotic second virial coefficient for BSA isslightly positive, increasing with ionic strength and pH. The osmotic second virialcross coefficient of the mixture lies between the coefficients for lysozyme andBSA, indicating that the attractive forces for a lysozyme—BSA pair areintermediate between those for the lysozyme—lysozyme and BSA—BSA pairs. For proteinconcentrations less than 100 g-L−1, experimental osmotic-pressure data comparefavorably with results from an adhesive hard-sphere model, which has previouslybeen shown to fit osmotic compressibilities of lysozyme solutions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005112927213
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Protein salting-out: Phase equilibria in two-protein systems (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 53 (1997), S. 567-574 
    Details
    ISSN: 0006-3592
    Keywords: salting out ; precipitation ; protein separation ; protein association ; lysozyme ; α-chymotrypsin ; ovalbumin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The phase behavior of two aqueous binary protein mixtures, lysozyme-chymotrypsin and lysozyme-ovalbumin, was determined in ammonium sulfate solutions. Protein concentrations were determined in both phases as a function of pH and ionic strength. For lysozyme-chymotrypsin mixtures, the observed phase behavior was similar to that for each individual protein; the presence of the second protein had little influence. The phase behavior of lysozyme-ovalbumin mixtures, however, was different from that of the respective single-protein systems. Lysozyme and ovalbumin are found together in egg whites; their association is both pH and ionic-strength dependent. The association of proteins is a key determinant of protein solubility in salt solutions. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 567-574, 1997.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 3
    Electronic Resource
    Electronic Resource
    Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 57 (1998), S. 11-21 
    Details
    ISSN: 0006-3592
    Keywords: proteins ; salts ; intermolecular interactions ; potentials of mean force ; precipitation ; crystallization ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Protein-protein and protein-salt interactions have been obtained for ovalbumin in solutions of ammonium sulfate and for lysozyme in solutions of ammonium sulfate, sodium chloride, potassium isothiocyanate, and potassium chloride. The two-body interactions between ovalbumin molecules in concentrated ammonium-sulfate solutions can be described by the DLVO potentials plus a potential that accounts for the decrease in free volume available to the protein due to the presence of the salt ions. The interaction between ovalbumin and ammonium sulfate is unfavorable, reflecting the kosmotropic nature of sulfate anions. Lysozyme-lysozyme interactions cannot be described by the above potentials because anion binding to lysozyme alters these interactions. Lysozyme-isothiocyanate complexes are strongly attractive due to electrostatic interactions resulting from bridging by the isothiocyanate ion. Lysozyme-lysozyme interactions in sulfate solutions are more repulsive than expected, possibly resulting from a larger excluded volume of a lysozyme-sulfate bound complex or perhaps, hydration forces between the lysozyme-sulfate complexes. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 57: 11-21, 1998.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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