Abstract
THE existence in human and animal serum of protein constituents which migrate during electrophoresis at rates faster than that of albumin has been widely reported in the literature by investigators using moving boundary electrophoresis1 and electrophoresis on paper2–5 and in hydrolysed starch-gels6,7. Using tris buffer (pH 8.9), which consists of tris-(hydroxymethyl)aminomethane, ethylenediamine tetraacetic acid (EDTA) and boric acid, Aronsson and Grönwall8 reported not only an enhanced separation of the protein constituents of human serum and the appearance of a pre-albumin component, but also a partial splitting of the albumin peak during electrophoresis in tris/boric acid buffers.
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McLOUGHLIN, J. Splitting of Serum Albumin during Electrophoresis on Paper. Nature 191, 1305–1306 (1961). https://doi.org/10.1038/1911305a0
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DOI: https://doi.org/10.1038/1911305a0
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