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Salting-out of lysozyme and ovalbumin from mixtures / Yu-Chia Cheng in Industrial & engineering chemistry research, Vol. 47 n°15 (Août 2008) 

Public ISBD [article]  in Industrial & engineering chemistry research > Vol. 47 n°15 (Août 2008) . - p. 5203–5213 Titre : Salting-out of lysozyme and ovalbumin from mixtures : predicting precipitation performance from protein-protein interactions Type de document : texte imprimé Auteurs : Yu-Chia Cheng, Auteur ; Carolina L. Bianco, Auteur ; Stanley I. Sandler, Auteur ; Abraham M. Lenhoff, Auteur Année de publication : 2008 Article en page(s) : p. 5203–5213 Note générale : Bibliogr. p. 5212-5213 Langues : Anglais (eng) Mots-clés : Protein−protein  interactions  --  ovalbumin;  Protein−protein  interactions  --  lysozyme;  Cross-interaction  chromatograph Résumé : Protein−protein interactions, whether desirable or not, can have direct effects on protein separations. The most obvious of these are interactions between similar molecules, which determine the thermodynamic properties and phase behavior of protein solutions. Interactions between dissimilar molecules also affect the properties and phase behavior of protein mixtures and, therefore, protein separations. Here, we seek to quantify these effects by comparing precipitation behavior from binary solutions with direct measurements of protein−protein interactions using cross-interaction chromatography, which is a variant of affinity chromatography that provides data that can be interpreted in terms of the virial cross-coefficient. First, the effects of pH, ionic strength, different precipitants and the initial protein concentrations and their ratio on the binary precipitation of lysozyme and ovalbumin were investigated. Next, self- and cross-interaction measurements were used to suggest the optimal precipitation conditions for separating lysozyme from ovalbumin. The results show that protein interactions can explain anomalies and inconsistencies that frequently confound the extraction of meaningful general trends in separations analyses. En ligne : http://pubs.acs.org/doi/abs/10.1021/ie071462p [article] Salting-out of lysozyme and ovalbumin from mixtures : predicting precipitation performance from protein-protein interactions [texte imprimé] / Yu-Chia Cheng, Auteur ; Carolina L. Bianco, Auteur ; Stanley I. Sandler, Auteur ; Abraham M. Lenhoff, Auteur . - 2008 . - p. 5203–5213. Bibliogr. p. 5212-5213 Langues : Anglais (eng) in Industrial & engineering chemistry research > Vol. 47 n°15 (Août 2008) . - p. 5203–5213 Mots-clés : Protein−protein  interactions  --  ovalbumin;  Protein−protein  interactions  --  lysozyme;  Cross-interaction  chromatograph Résumé : Protein−protein interactions, whether desirable or not, can have direct effects on protein separations. The most obvious of these are interactions between similar molecules, which determine the thermodynamic properties and phase behavior of protein solutions. Interactions between dissimilar molecules also affect the properties and phase behavior of protein mixtures and, therefore, protein separations. Here, we seek to quantify these effects by comparing precipitation behavior from binary solutions with direct measurements of protein−protein interactions using cross-interaction chromatography, which is a variant of affinity chromatography that provides data that can be interpreted in terms of the virial cross-coefficient. First, the effects of pH, ionic strength, different precipitants and the initial protein concentrations and their ratio on the binary precipitation of lysozyme and ovalbumin were investigated. Next, self- and cross-interaction measurements were used to suggest the optimal precipitation conditions for separating lysozyme from ovalbumin. The results show that protein interactions can explain anomalies and inconsistencies that frequently confound the extraction of meaningful general trends in separations analyses. En ligne : http://pubs.acs.org/doi/abs/10.1021/ie071462p