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通过肌球蛋白轻链磷酸化对果蝇肌球蛋白ATP酶活性的调节——I. 野生型果蝇

Regulation of Drosophila myosin ATPase activity by phosphorylation of myosin light chains--I. Wild-type fly.

作者信息

Takahashi S, Takano-Ohmuro H, Maruyama K

机构信息

Department of Biology, Faculty of Science, Chiba University, Japan.

出版信息

Comp Biochem Physiol B. 1990;95(1):179-81. doi: 10.1016/0305-0491(90)90267-w.

DOI:10.1016/0305-0491(90)90267-w
PMID:2139597
Abstract
  1. Two types of myosins with phosphorylated and dephosphorylated myosin light chains were prepared from Drosophila flies. The former had ATPase (Ca2(+)- and Mg2(+)-activited) activities twice those of the latter. 2. The myosin phosphorylated with crude myosin light chain kinase from flies showed ATPase (Ca2(+)- and Mg2(+)-activated) activaties twice those of the dephosphorylated myosin. 3. It is suggested that phosphorylation of myosin light chains several hours after emergence stimulates myosin ATPase activity so as to facilitate the flight function of the fruitfly.
摘要
  1. 从果蝇中制备了两种分别带有磷酸化和去磷酸化肌球蛋白轻链的肌球蛋白。前者的ATP酶(Ca2+和Mg2+激活型)活性是后者的两倍。2. 用果蝇的粗肌球蛋白轻链激酶磷酸化的肌球蛋白,其ATP酶(Ca2+和Mg2+激活型)活性是去磷酸化肌球蛋白的两倍。3. 这表明羽化后数小时肌球蛋白轻链的磷酸化刺激了肌球蛋白ATP酶活性,从而促进果蝇的飞行功能。

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