Osmotic pressure measurements of ovalbumin and lysozyme mixtures.
Ovalbumin and lysozyme have been reported to undergo a mixed association in solutions of low ionic strength. Osmotic pressure experiments were performed on ovalbumin and on lysozyme solutions in 0.06 M cacodylate buffer (I = 0.02, pH = 5.8) at 30 and at 37 degrees C. The individual proteins did not undergo any self-associations at either temperature; these measurements indicated that each of the solutions was nonideal. Osmotic pressure experiments on three blends of lysozyme and ovalbumin at 30 and 37 degrees C could be interpreted in two ways. One interpretation was that a nonideal, nonassociating mixture of A and B was present; for the three solutions the mixed nonideal term BAB was negative. A negative nonideal term is usually interpreted as indicating an association. The other interpretation of the data was as a quasi-ideal mixed association of the type A + B in equilibrium AB.
McCarty
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BW
Chemistry Department, Texas A&M University, College Station 77843.
Adams
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ET
D002849:Chromatography, Gas; D008567:Membranes, Artificial; D009113:Muramidase / Q000032:analysis*; D009994:Osmolar Concentration; D010047:Ovalbumin / Q000032:analysis*; D013056:Spectrophotometry, Ultraviolet; D014461:Ultracentrifugation
D008567:Membranes, Artificial; D010047:Ovalbumin; D009113:Muramidase