Polymerization of Acetylated Lysozyme and Impairment of Their Amino Acid Residues Due to α-Dicarbonyl and α-Hydroxycarbonyl Compounds

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Abstract
We studied the mechanism of polymerization of proteins induced by storage with reducing sugars. Glucose alone did not polymerize acetylated lysozyme as a solid (75% relative humidity), but it did when there was free Lys. This indicated that a certain substance generated through a reaction between glucose and amino groups of proteins polymerized the proteins. The substance impaired Arg residues. The impaired Arg residues appeared in three peaks eluting just behind the Phe peak on amino acid analysis. .alpha.-dicarbonyl and .alpha.-hydroxycarbonyl compounds such as 2,3-butanedione, glyoxal, methylglyoxal, dihydroxyacetone, glyceraldehyde, and glycolaldehyde polymerized both lysozyme and acetylated lysozyme, and impaired their Arg residues. However, the elution patterns of the impaired amino acid residues on amino acid analysis were different from that observed with glucose. Glyoxal, methylglyoxal, and 2,3-butanedione polymerized proteins to a notable extent even under the conditions used conventionally for chemical modification of Arg residues.

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