The valences of protein ions from electrophoretic and membrane potential measurements

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Abstract
Measurements were made in acetate and phosphate buffers of the variations in size of the [delta] -boundary formed during the electrophoresis of horse serum albumin A with modified concns. of buffer salts in the supernatant fluid. The valences of the protein ions calculated from these observations were compared with those deduced from mobility and membrane potential measurements. The last two methods compare very favorably, but the first gives rather higher values. The reasons for this are discussed.