In vitro Dimerization of I-protein, an A-I Junctional Component of Skeletal Muscle Myofibrils : Biochemistry
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概要
- 論文の詳細を見る
Chicken myofibrillar I-protein, which was purified using ammonium sulfate precipitation and DEAE-cellulose column chromatography, was separated into two fractions by gel filtration, disc alkaline electrophoresis, or SDS polyacrylamide gel electrophoresis without SH reagents. These fractions consisted of 100,000 dalton and 50,000 dalton components. The amount of the high molecular weight component increased under the oxidizing conditions, while the amount of the low one increased when SH reagents were added. On the other hand, antiserum raised against 50,000 dalton component reacted with both of them, as revealed by immunoelectrophoresis. Therefore, it is concluded that I-protein dimerizes under oxidizing solutions. However, dimeric I-protein did not inhibit the ATPase activity of actomyosin in vitro, whereas monomeric I-protein did.
- 社団法人日本動物学会の論文
- 1988-04-15
著者
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Ohashi Kazuaki
Graduate School of Pharmaceutical Sciences, The University of Tokyo
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Maruyama Koscak
Department of Biology, Faculty of Science, Chiba University
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Maruyama K
Laboratory Animal Development And Research Group National Institute Of Radiological Sciences
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Tsuneoka Makoto
Department Of Biology Faculty Of Science Chiba University:(present)department Of Physiology Kansai M
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Ohashi Kazuyo
Department Of Biology Faculty Of Science Chiba University
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Maruyama Koscak
Department Of Biology Faculty Of Science Chiba University
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