Aminosäuren aus Eiweißhydrolysaten. Kurze Mitteilung

Abstract

A preliminary report outlining in a general way the application of the principles of chromatographic adsorption in the fractionation of the amino acids of protein hydrolyzates by adsorption on C activated with H2S. Amino acids strongly adsorbed from 2 N aq. HCl soln. at [long dash]10[degree]-0[degree] could be eluted with NHS or an alkaline acetone soln. Hydrochlorides of weakly adsorbed amino acids could be separated on the activated C by using alcohol-acetone as the solvent and developing agent. When the residues, obtained upon concentrating to dryness the fractionally collected filtrates which had passed through the C, were dissolved in alcohol, some of the amino acids (glutamic acid, lysine, histidine) crystallized out as the hydrochlorides, either at once or after acetone was added. Arginine was obtained as the di-HCl and converted to the mono-HCl by adding aniline to its alcoholic soln. Several mono-amino acids (leucine, isoleucine, nor-leucine) could also be crystallized as the hydrochlorides upon the addition of a large amt. of acetone or pptd. as the free amino acids upon adding aniline to the alcoholic soln.