Abstract
GILBERT1 developed a differential gel chromatographic technique to compare the extents of association of two different haemoglobin species. This entailed the layering of a relatively large volume of solution of one species onto a column equilibrated with an identical concentration of the other. Differences in the weight-average elution volumes of the two solutes resulted in a change of protein concentration at the junction of the two solutions, this effect being a consequence of mass conservation. We wish to explore Gilbert's suggestion1 that the differential method could be adapted to study the effects of environmental factors (pH and ionic strength, I) on the state of a single solute system. The acid expansion of bovine serum albumin provides an example where a variation in pH induces a change in conformation and thus in elution volume. The effect of ionic strength on the extent of association of β-lactoglobulin A has also been studied, the change of weight-average elution volume in this instance being used to compare the association constants pertinent to two environments of different ionic strength.
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BAGHURST, P., NICHOL, L., RICHARDS, R. et al. Differential Chromatographic Study of Macromolecular Changes governed by Environmental Factors. Nature 234, 299–301 (1971). https://doi.org/10.1038/234299a0
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DOI: https://doi.org/10.1038/234299a0
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