By M. L.; Edsall, John T. (Eds) Anson
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Extra resources for Advances in protein chemistry Volume 2
Thus the two methods may well be of value when used together. For large scale separations ionophoresis is obviously the more convenient if a suitable diaphragm apparatus can be used. 5. PRECIPITATION METHODS: THE W O R K OF B E R Q M A " AND COLLEAQUEB For isolating particular amino acids or groups of amino acids not many new precipitants have been introduced during the last fifteen years by workers other than the Bergmann group, whose work is separately discussed below. Nitranilic acid and cuprous oxide have now definitely established themselves beside the traditional reagents for quantitative work.
Thus the stoichiometric concentration of the anion (S-) of such a sulfonic acid may be considered equal to the concentration of the added sulfonic acid or of its sodium salt. If the pH of the system is sufficiently acid, so that a11 of the amino acid being preripitated is in the form of the cation (A+), then the solubility product of the slightly soluble salt (A%-) should be well defined in a given medium, and should be nearly independent of moderate variations in pFI, provided that the concentrations of other compononh in the system are held practirally constant.
Errors from these sources may to some extent be offset by determining correction-factors with known mixtures of amino acids. The method has been used for the analysis of wool (248, 249), gelatin ANALYTICAL CHEMISTRY OF THE PROTEINS 29 (249, 253)) gramicidin (252, 256)) tyrocidine (250), myosin and fibsin (173s)) and in studying hydrolysis products of methylated proteins ( 2 5 i , 258). Quite recently it has been used for analyzing ‘gramicidin S’ (10%). Dakin’s widely used method of butanol extraction for the separation of monoamino-monocarboxylic acids from the rest has been shown not to be very specific (259, 260).
Advances in protein chemistry Volume 2 by M. L.; Edsall, John T. (Eds) Anson