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By M. L.; Edsall, John T. (Eds) Anson
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Extra resources for Advances in protein chemistry Volume 2
The quantity of material required is remarkably small. 4 mg. Df protein is required for each 2-dimensional sheet and less for a l-dimensional experiment. 1 pg. of amino acid gives a clearly visible spot with ninhydrin. The method has not yet been made quantitative, but is already most useful qualitatively. 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.
Proline phosphotungstate is somewhat insoluble, and has been used (328) for purifying proline. FEavianic Acid This acid has been employed for precipitating arginine with considerable success. It was introduced by Kossel and Gross (329; cf. 330), who also studied the properties of the flavianates of a number of other bases. It has found widespread use as an almost quantitative precipitant of arginine from complete protein hydrolyzates as its monoflavianate, and in the later stages of determining arginine by other methods.
Some other amino acids reduce periodate, but neither NH3 nor volatile aldehydes are liberated (472, 412). The aldehydo-acids which are supposedly formed at the same time have not so far been much studied (cf. 437). Threonine gives acetaldehyde on treatment with periodate. This may readily be separated from the formaldehyde resulting from serine, hydroxylysine, etc. by vaporization in a stream of gas at low temperature. This forms the basis of Shinn and Nicolet’s (473; cf. 411) method for determin- 50 A.