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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 asl-and^-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. Alkali treatment has been used not only in traditional food processing and cooking,1~4) but also in modern food industry.5) Noting the decrease of cysteine on the alkali treatment of protein, Bohak6) first isolated a cross-linked amino acid, Ar£-(DL-2-amino-2-carboxyethyl)