1. 1. Four proteins of known sequence (lysozyme, myoglobin, ribonuclease and insulin) have been treated with NaOH and ammonia solutions, and the amounts of lysinoalanine and β-aminoalanine estimated in the hydrolysates by high-voltage paper electrophoresis. The relative amounts of each amino acid are explained by reference to the positions of cystine and serine residues in relation to lysine residues and amide side-chains in the proteins. 2. 2. The evidence indicates that β-aminoalanine is formed by direct addition of ammonia to α-aminoacrylic acid residues, and not by initial formation of a cross-link between α-aminoacrylic acid and asparagine or glutamine residues. 3. 3. Further evidence has been found for the formation of α-aminoacrylic acid from residues other than cystine, by treatment of myoglobin with alkali. 4. 4. Treatment of β-lactoglobulin and wheat gluten, whose sequences are unknown, has enabled tentative suggestions to be made about the relative positions of certain residues in these proteins. © 1969.