Purification of Actin Based Motor Protein from Chara corallina.

DOI Web Site 被引用文献30件 オープンアクセス

書誌事項

公開日
1994
DOI
  • 10.2183/pjab.70.175
公開者
日本学士院

この論文をさがす

説明

Actin based motor protein was purified from Chara corallina using high performance liquid chromatography. Sodium dodecyl sulfate gel electrophoresis showed that the molecular weight of the main band was about 230kDa. Although the molecular weight was quite similar to that of the heavy chain of muscle myosin (myosin II), the motor protein was soluble at low ionic strength and antibody raised against the main band did not recognize smooth muscle myosin. The antibody also did not recognize the actin based motor protein from lily pollen tube. The motor protein translocated fluorescently labeled actin filaments at about 25μm/s in the in vitro motility assay. The MgATPase activity of the motor protein was enhanced by F-actin about 150 fold. Calcium ion concentration had little effect on both the motor activity and the actin activated MgATPase activity.

収録刊行物

被引用文献 (30)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ