STUDIES ON PROTEIN MULTIMERS:

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Abstract
β‐Galactosidase from E. coli dissociates readily in commonly used buffer systems except at pH values close to the isoelectric point. Dissociation of the tetramer to the monomer does not result, per se, in a substantial change in the value of the apparent specific volume. In contrast, dissociation of very dilute protein solutions such as those produced at the meniscus in high speed sedimentation equilibrium runs, or dissociation of protein at low ionic strength, does lead to monomeric forms with a lower apparent specific volume. The ϕ2 value of the monomer formed in 90% glycerol changes markedly on transfer from aqueous buffer to 99.8% D2O. The dissociation of the tetrameric form of β‐galactosidase in aqueous buffer is minimized by 99.8% D2O.