Abstract
An account is given of an investigation of the influence of dry heat on wool keratin. It is shown by three different chemical techniques that cross-linking occurs up to a temperature at which the amino-acid decomposition becomes marked. Although Iysinoalanine and lanthionine are shown to be formed, these amino acids do not appear to be major contributors to the cross-linking of the heated protein. The covalent binding of the ∊-amino group of lysine was determined quantitatively, and, from the results obtained, it is deduced that this group is involved to a large extent in the formation of cross-links. On the basis of these findings, it is postulated that amide cross-links are formed through the ∊-amino group of lysine by reaction with carboxylic side chains of aspartic or glutamic acids or their amide derivatives.
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