Abstract
Traditionally, the charge of a protein molecule as determined by electrophoresis has been compared to that revealed by pH titration, and any lack of coincidence has been ascribed to ion binding, and the two results have been brought into agreement by adjustment of binding parameters (1). Metallo-thionein allows a unique opportunity to examine the validity of the electrophoretic approach, since the amino acid sequence and metal atom binding studies allow the absolute charge of the molecule to be computed (2). This then can be compared to the charge determined from electrophoretic mobility measurements to allow evaluation of the theories relating charge to mobility.
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Bethune, J.L., Budreau, A.J., Kägi, J.H.R., Vallee, B.L. (1979). Determination of the Charge of Horse Kidney Metallothionein by Free Boundary Electrophoresis. In: Kägi, J.H.R., Nordberg, M. (eds) Metallothionein. Experientia Supplementum, vol 34. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-6493-0_13
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DOI: https://doi.org/10.1007/978-3-0348-6493-0_13
Publisher Name: Birkhäuser, Basel
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Online ISBN: 978-3-0348-6493-0
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