Recently a method has been described (Fromageot, Jutisz and Lederer, 1948) of fractionating amino acids and eventually peptides arising from protein hydrolysis, into the following groups: basic substances, acidic substances and aromatic neutral substances, separated by adsorption on silica gel, “acidic” alumina and activated charcoal respectively, and non-adsorbed non-aromatic neutral substances. In each case, elution of adsorbed substances permits their quantitative recovery. Such a method constitutes a first series of separations preliminary either to further separations permitting individual isolations, as in the excellent methods of Stein and Moore and of Craig, Gregory and Barry, described in this Symposium, or to specific chemical titrations of each of the amino acids and peptides in each of the groups thus isolated. It seems, indeed, that owing to the great number of amino acids and peptides bound to coexist in one hydrolysate, such a preliminary step is necessary to avoid overlapping in the subsequent
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C. Fromageot (1950) studied this question.