By M. L.; Edsall, John T. (Eds) Anson
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Extra resources for Advances in protein chemistry Volume 2
Under these conditions deamination of amino acids occurs at the cathode unless the current density there is kept very low. Only the amino acids go to the cathode compartment. Gordon, Martin, and Synge (282, 283) have used the 3-compartment cell to study the basic andneutral fractions of partial hydrolyzates of proteins. A number of other workers have used the same arrangement (284-289s). Ruppel (290, 291) and colleagues, using chromed gelatin as anode membrane and parchment paper as cathode membrane, used a 3-compartment cell to electrodialyze electrolytes from serum.
Cf. ) Synge (256) has used partition chromatography on raw potato starch with n-butanol as a preparative method, using ordinary chromatograni tubes. Here again the starch has been shown to act merely as a mechanical support for the water phase. Hence information as to the behavior of materials gained upon paper should be available for prediction of their behavior upon starch, and vice versa. Wieland and Fremerey (264a) have employed partition chromatography with silica gel in phenol-chloroform-water and similar systems for separating the Cu ‘salts’ of monoamino acids.
1-4 volt/cm is applied for 24-48 hrs. A ‘print’ may be taken from the slab when required by laying a strip of dry filter-paper on it. Ninhydrin shows the location of the amino acids. Buffer in the gel is necessary since where the pH is such that a given substance is partially ionized, ionophoresis will result in pH changes, since ions are moved and then de-ionize and neutral molecules are left behind, some of which then ionize. Since the buffer behaves similarly if suitably chosen, no pH changes need result in the presence of buffer.
Advances in protein chemistry Volume 2 by M. L.; Edsall, John T. (Eds) Anson