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Protein salting-out: Phase equilibria in two-protein systems

✍ Scribed by C. J. Coen; J. M. Prausnitz; H. W. Blanch

Publisher: John Wiley and Sons
Year: 1997
Tongue: English
Weight: 262 KB
Volume: 53
Category: Article
ISSN: 0006-3592
DOI: 10.1002/(sici)1097-0290(19970320)53:6<567::aid-bit4>3.0.co;2-k

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✦ Synopsis

The phase behavior of two aqueous binary protein mixtures, lysozyme-chymotrypsin and lysozymeovalbumin, 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 singleprotein 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.

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