Freezing of actin. reversible oxidation of a sulfhydryl group and structural change

Shin'ichi Ishiwata*


研究成果: Article査読

23 被引用数 (Scopus)


It was found that the essential change in actin (whether G- or F-actin) on freeze-thawing was the specific oxidation of one of five sulfhydryl (SH) groups, i.e. The SH group of Cys 373 in the amino acid sequence. Oxidized SH groups formed an inter-molecular disulfide (SS) bond to yield an actin dimer. F-actin, subjected to freeze-thawing (or F-actin obtained by the transformation of once frozen G-actin which is essentially a dimer), has anomalous physico-chemical properties and a different conformation from normal F-actin, as determined by optical and electron microscopic observations, as well as high steady ATP-splitting activity in the presence of Mg2+. However, it was found that those peculiarities disappeared and normal actin was reformed on reducing the oxidized SH group with dithiothreitol (DTT). It was also found that the normal characteristics of actin were preserved for more than four months on freezing in the presence of a sufficient amount of DTT.

ジャーナルJournal of Biochemistry
出版ステータスPublished - 1976 9月

ASJC Scopus subject areas

  • 統計学、確率および不確実性
  • 応用数学
  • 生理学(医学)
  • 放射線学、核医学およびイメージング
  • 分子生物学
  • 生化学


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