Identification and properties of reactive sites in protein capable of binding carbon dioxide in a gas-solid phase system.

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Abstract
In order to identify the functional groups which really con-tribute to the carbon dioxide gas adsorption by proteins, ε-amino groups of lysine residues of egg albumin were chemically modified with trinitro-benzene sulfonic acid to various degrees. About 60% of the total amount of carbon dioxide gas adsorbed by solid egg albumin diminished by complete modification. The amount of carbon dioxide gas adsorbed by lysozyme, its hydro-lyzates and gelatin hydrolyzates depended upon the lysine content, arginine content and average molecular weight. The good correlation was obtained between the amount of carbon dioxide gas adsorbed and the total of lysine and arginine content of them. The ability of carbon dioxide gas adsorption by α-amino group of amino acids and oligopeptides was found to be developed by the elongation of the peptide chain of glycine and other amino acid, by the removal of α-carboxyl group of histidine and tyrosine to corresponding amines and by the esterification of α-carboxyl group of leucine with p-nitrophenol. These results clearly indicate that CO2 binding sites in protein in the gas-solid phase system are ε-amino, α-amino and guanidinium groups.

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