A gas-liquid chromatographic method was explored for the analysis of lanthionine and lysinoalanine as well as lysine, cystine, and S -carboxyethylcysteine in chemically modified wool samples. The amino acids in the wool hydrolyzate were converted to n-butyl esters of N-trifluoroacetyl derivatives according to the method of Gehrke et al. The retention indices of the five amino acids mentioned above as well as other protein amino acids such as proline, phenytalanine, histidine (as mono and diacyl derivatives), tyrosine, arginine, and tryptophane were determined on OV-17 and Dexsil 300 GC. It was found that Dexsil 300 GC was suitable for the intended analysis with n-butyl stearate as an internal standard. The molar responses of these amino acids were determined.
The reaction of Merino wool fibers with aqueous KCN was studied. The cystine (CYS) and lanthionine (LAN) contents in the hydrolysates of wool samples were determined by the gas chro matographic method. The CYS content decreased and the LAN content increased with the treating time. The sum of CYS and LAN contents, that is, the total crosslink content, decreased to a minimum and returned to the original value as the reaction progressed. In order to see the effect of organic solvents on the reaction of wool with KCN, Merino wool fibers were treated with KCN in 3:1 (v/v) mixtures of water and organic solvents. LAN was formed more when wool fibers were treated in the presence of organic solvents such as n-propanol than when wool fibers were treated in water. The wool fabrics treated with KCN in the presence of organic solvents were much stiffer than those treated in the absence of organic solvents and had pin holes through which light passed. It was observed by scanning electron micrography that the yarns in the treated fabric in the presence of n-propanol, were more dense and the constituting fibers were more oriented. There appeared many lengthwise wrinkles on the surface of the treated fibers.
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