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Protein—Protein Interactions in Aqueous Ammonium Sulfate Solutions. Lysozyme and Bovine Serum Albumin (BSA) (2000)

Moon, Y. U. ; Curtis, R. A. ; Anderson, C. O. ; [et al.]

Springer

Journal of solution chemistry 29 (2000), S. 699-718

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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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The effect of aqueous surfactant solutions on alcohol dehydrogenase (LADH) (1993)

Creagh, A. L. ; Prausnitz, J. M. ; Blanch, H. W.

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 41 (1993), S. 156-161

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ISSN: 0006-3592

Keywords: LADH ; surfactants ; ERP ; CD ; fluorescence ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: Alcohol dehydrogenase (LADH) was studied in aqueous solutions of surfactants to determine its structural and catalytic characteristics. Fluorescence, circular dichroism (CD), and electron paramagnetic resonance (ERP) techniques were used to study structural changes to the enzyme. The activity of LADH in catalyzing the oxidation of ethanol was investigated. Short-chain alkyl sulfonates and sulfates did not deactivate LADH or alter its structure. Longer and branched alkyl sulfates and sulfonates, as well as a cationic surfactant (CTAB), affected both LADH activity and conformation. © 1993 John Wiley & Sons, Inc.

Additional Material: 6 Ill.