Limits and Sites of Lysinoalanine Formation in Lysozyme, α-Lactalbumin and αs1- and β-Caseins by Alkali Treatment

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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 α-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 αsl- 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 α-lactalbumin and caseins.

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