Myosin electrophoretic mobilities

That the electrophoretic mobility is independent of the nature and concentration of the above ions, and depends solely on pH, is almost conclusive proof that the charge on L-myosin particles is determined exclusively by the binding (and release) of H ions. This means that the other ions, including sodium and potassium, are not bound, but are free in solution as gegenions. The agreement between the alkali content of salt-free myosin gel and the amount of protons given up on the alkaline side of the I.P. leads to the same conclusion (Hollwede and Weber, 1938) and finally, the pH-mobility curve found by Erdos and Snellman (1948)... 

Fig. 16. Electrophoretic mobility and H+ binding of L-myosin. pH titration curve from Dubuisson, 1941 - - mobility from Dubpisson (1946b, 1948b, and 1950b) (c/. Table VIII) mobility from Erdos and Snellman (1948).

Fig. 17. Electrophoretic mobility—pH curve of L-myosin in varying concentrations of calcium and magnesium chlorides (0.03 — 0.24 M). O < 0.1 M salt A > 0.1 M. salt (after Erdos and Snellman, 1948).

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