Additivity of the Sliding Velocity of Acto-H-meromyosin in vitro Driven by ATP and GTP.

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概要

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• The in vitro motility assay of the sliding velocity of acto-H-meromyosin driven by ATP and GTP was made according to the previous method.1) In the presence of 15μM ATP (and in the absence of ATP regenerating system), the sliding velocity of the F-actin labeled with rhodamine-phalloidin decreased gradually as the consumption of the added ATP proceeded. When GTP (2mM) was added together with ATP (15μM), the sliding velocity of the labeled F-actin at initial stage was approximately equal to the sum of the individual contributions of GTP and ATP. Strikingly, however, the sliding velocity of the labeled F-actin in the presence of ATP and GTP did not show any decrease at least until 6min. This means that the sliding velocity of the labeled F-actin exceeds the simple sum of the contributions of ATP and GTP. The phenomenon is very difficult to explain in terms of the current ideas on the sliding mechanism of actomyosin.

• 日本学士院の論文

著者

• Oda Toshiro

  Department Of Urology Hakodate Goryoukaku Hospital

• Mihashi Koshin

  Department Of Physics Faculty Of Science Nagoya University

• ODA Toshiro

  Department of Physics, Faculty of Science, Nagoya University

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• Additivity of the Sliding Velocity of Acto-H-meromyosin in vitro Driven by ATP and GTP.

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