Diastereomers of methionine S-oxide in the hinge-ligament proteins of molluscan bivalve species.

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概要

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• The diastereomer ratio was analyzed on methionine <I>S</I>-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 <I>S</I>-oxide. The methionine <I>S</I>-oxide was released from the protein by proteolytic digestions and was found to be a mixture of approximately equall amounts of two diastereomers, (5<I>S</I>)- and (5<I>R</I>)-L-methionine <I>S</I>-oxide.

• 公益社団法人 日本化学会の論文

著者

• Kikuchi Yasuo

  Department Of Biomolecular Sciences Graduate School Of Life Science Tohoku University

• Tamiya Nobuo

  Department of Chemistry, Faculty of Science, Tohoku University

• Higashi Kiyoshi

  Department of Chemistry, Faculty of Science, Tohoku University

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