Adenylate deaminase binding to synthetic thick filaments of myosin.
Adenylate deaminase binding to synthetic thick filaments of myosin.
复制标题
腺苷酸脱氨酶与合成的肌球蛋白粗丝结合。
DOI：
10.1073/pnas.77.12.7186
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发表时间：
1980
影响因子：
11.1
通讯作者：
Frieden,C
中科院分区：
文献类型：
--
作者：
Koretz,JF;Frieden,C
腺苷酸脱氨酶（AMP脱氨酶; AMP氨基水解酶，EC 3.5.4.6）是一种在骨骼肌中以特别高的浓度发现的四聚体酶，先前已显示在体外与肌球蛋白的亚片段-2-部分强烈结合，在体内与A带的末端强烈结合。它在这里示出，当腺苷酸脱氨酶与骨骼肌球蛋白在pH 7.0的合成丝的形成过程中透析，它装饰的丝在14.3 nm的间隔，大概是在该地区暴露的骨干之间的crossbridge水平。聚集体的光学衍射揭示了由肌球蛋白组织引起的反射的增强和由细丝表面上的腺苷酸脱氨酶排列引起的其他反射。腺苷酸脱氨酶可作为肌球蛋白存在和组织研究中的特异性标记。
Adenylate deaminase (AMP deaminase; AMP aminohydrolase, EC 3.5.4.6), a tetrameric enzyme found at particularly high concentrations in skeletal muscle, has previously been shown to bind strongly to the subfragment-2-portion of myosin in vitro and to the ends of the A band in vivo. It is shown here that when adenylate deaminase is dialyzed with skeletal myosin during formation of synthetic filaments at pH 7.0 it decorates the filament at 14.3-nm intervals, presumably in the region of exposed backbone between crossbridge levels. Optical diffraction of the aggregates reveals both enhancement of reflections arising from underlying myosin organization and other reflections arising from adenylate deaminase arrangement on the filament surface. Adenylate deaminase can thus be used as a specific label in the study of myosin presence and organization.