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Chromatographic measurement of protein-protein interactions

Record Type:	Electronic resources : Monograph/item
Title/Author:	Chromatographic measurement of protein-protein interactions
Author:	Teske, Christopher Alan.
Description:	97 p.
Notes:	Chairs: Harvey W. Blanch; John M. Prausnitz.
Notes:	Source: Dissertation Abstracts International, Volume: 65-02, Section: B, page: 0891.
Contained By:	Dissertation Abstracts International65-02B.
Subject:	Engineering, Chemical.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3121725
ISBN:	0496690760

Chromatographic measurement of protein-protein interactions
Teske, Christopher Alan.

Chromatographic measurement of protein-protein interactions [electronic resource] - 97 p.

Chairs: Harvey W. Blanch; John M. Prausnitz.

Thesis (Ph.D.)--University of California, Berkeley, 2003.

To measure protein-protein interactions chromatographically, one protein is immobilized on a porous stationary phase while a solution of the second protein passes through the column as the mobile phase. The retention time of the mobile protein (relative to that of a similarly-sized non-interacting tracer) provides a quantitative measure of the mobile-protein/immobile-protein interaction. Chromatographic measurement of protein-protein interactions requires significantly less protein than static light scattering or membrane osmometry and, in principle, can directly measure interactions between unlike proteins.

ISBN: 0496690760Subjects--Topical Terms:

226989
Engineering, Chemical.

Chromatographic measurement of protein-protein interactions
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245 1 0 $a Chromatographic measurement of protein-protein interactions $h [electronic resource]
300 $a 97 p.
500 $a Chairs: Harvey W. Blanch; John M. Prausnitz.
500 $a Source: Dissertation Abstracts International, Volume: 65-02, Section: B, page: 0891.
502 $a Thesis (Ph.D.)--University of California, Berkeley, 2003.
520 # $a To measure protein-protein interactions chromatographically, one protein is immobilized on a porous stationary phase while a solution of the second protein passes through the column as the mobile phase. The retention time of the mobile protein (relative to that of a similarly-sized non-interacting tracer) provides a quantitative measure of the mobile-protein/immobile-protein interaction. Chromatographic measurement of protein-protein interactions requires significantly less protein than static light scattering or membrane osmometry and, in principle, can directly measure interactions between unlike proteins.
520 # $a Understanding how solution conditions affect protein-protein interactions is useful for designing and optimizing protein separation processes such as salt-induced protein precipitation. Further, attractive protein-protein interactions can lead to protein aggregation which has been linked to Alzheimer's and Parkinson's disease. Information for interactions between unlike proteins is necessary for predicting phase equilibria for multi-component protein solutions commonly encountered in protein-purification processes. Common methods for measuring protein-protein interactions include static light scattering, membrane osmometry and equilibrium sedimentation. These methods suffer from the disadvantage of requiring a relatively large amount of protein. Further, with these techniques it is difficult to measure directly interactions between unlike proteins. Chromatographic measurement of protein-protein interactions provides a possible method to overcome these disadvantages.
520 # $a Using a standard liquid chromatograph, we have measured lysozyme-lysozyme interactions as a function of aqueous solution conditions (pH, ionic strength, salt identity). All measurements were at 25°C. Results are reported at pH 4 and 7 for sodium chloride (concentrations up to 1.7m) and ammonium sulfate (concentrations up to 1.0m). Osmotic second virial coefficients are calculated from our chromatographic results and compared with those from static light scattering. For reduction of chromatographic data, it is necessary to consider multibody interactions between a mobile lysozyme molecule and many immobilized molecules on the solid support. A model is constructed to account for multibody interactions assuming pairwise additivity and using a potential of mean force that contains hard sphere, electrostatic, and square-well contributions. (Abstract shortened by UMI.)
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773 0 # $g 65-02B. $t Dissertation Abstracts International
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790 1 0 $a Blanch, Harvey W., $e advisor
790 1 0 $a Prausnitz, John M., $e advisor
791 $a Ph.D.
792 $a 2003
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