Abstract
Abstract The role of the arginyl residues of κ-casein in α s1 -κ-casein complex formation was investigated by modifying with peptidyl arginine deiminase. The action of deiminase resulted in all five arginyl residues of κ-casein, which are located in the hydrophobic para-κ-casein region, being converted to uncharged citrullyl residues. This treatment resulted in loss of ability to stabilize α s1 -casein against calcium-induced precipitation. Deiminated κ-casein could not form a complex with α s1 -casein, but formed a polymer larger than the native one in spite of the presence of dithiotreitol. This suggests that the polymer of deiminated κ-casein could not dissociate into the smaller polymers necessary to form a complex with α s1 -casein. The role of the positive charge of arginine might be to interfere with further polymerization of κ-casein via hydrophobic interactions in the normal protein.
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