Abstract
Lysinoalanine was determined by gas chromatography. Lysinoalanine formation in lysozyme depended on alkali concentration, pH, temperature and exposure time. The upper limits of lysinoalanine formation in lysozyme and a-lactalbumin were related to the number of lysine residues with a cystine disulfide bond in the adjacent position rather than the individual contents of these residues. In cases of αs1- and β-caseins, the upper limits were related to the number of phosphoserine residues, regardless of their sequential relationship to lysine residues. Gel electrophoresis suggested that intermolecular cross-linking took place in the a-lactalbumin and caseins.
