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dc.contributor.advisorReid, Robert O.
dc.creatorSarquis, Jerry Leon
dc.description.abstractThe self-association of [beta]-lactoglobulin C at acid pH has been studied in glycine buffers and acetate buffers by sedimentation equilibrium. In glycine buffers, pH ca. .25, the self-association was studied by low and high speed sedimentation equilibrium experiments at four temperatures, 10, 16, 20 and 25 [degrees] C. One buffer had an ionic strength of 0.1 and the other had an ionic strength of 0.2. With either buffer, the concentration dependence of the apparent weight average molecular weight, M[subscript wa], was characteristic of a nonideal self-association. Like its genetic variants, [beta]-lactoglobulins A and B, the self-association of [beta]-lactoglobulin C increased with decreasing temperature. At the same temperature, the association was always stronger in the buffer having the higher ionic strength. Several models were used to test the self-association, and a monomer-dimer self-association seemed to describe the self-association best with either buffer. Values of the association equilibrium constant, K[subscript 2], ranged from 27.2 to 5.9 dl/g at I = 0.1 and from 60.1 to 27.2 dl/g at I = 0.2.en
dc.format.extent122 leavesen
dc.rightsThis thesis was part of a retrospective digitization project authorized by the Texas A&M University Libraries. Copyright remains vested with the author(s). It is the user's responsibility to secure permission from the copyright holder(s) for re-use of the work beyond the provision of Fair Use.en
dc.subject.classification1974 Dissertation S246
dc.titleSedimentation equilibrium studies on betalactoglobulin C at acid pHen
dc.typeThesisen A&M Universityen of Philosophyen
dc.format.digitalOriginreformatted digitalen
dc.publisher.digitalTexas A&M University. Libraries

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