Diastereomers of Methionine S-Oxide in the Hinge-Ligament Proteins of Molluscan Bivalve Species

Article abstract of DOI:10.1246/bcsj.61.2083

The diastereomer ratio was analyzed on methionine S-oxide residues formed by in vivo posttranslational oxidation of methionine residues in a protein.The hinge-ligament protein of molluscan bivalves is distinct from usual proteins in containing a large amount of methionine S-oxide.The methionine S-oxide was released from the protein by proteolytic digestions and was found to be a mixture of approximately equall amounts of two diastereomers, (5S)- and (5R)-L-methionine S-oxide.