Spectroscopic studies on invertebrate myosins and light chains.
Spectroscopic studies on invertebrate myosins and light chains.
复制标题
无脊椎动物肌球蛋白和轻链的光谱研究。
DOI：
10.1021/bi00618a018
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发表时间：
1978
期刊：
影响因子：
2.9
通讯作者：
A. Szent
中科院分区：
文献类型：
--
作者：
P. Chantler;A. Szent
从14块无脊椎动物肌肉中分离出肌球蛋白，所有肌肉都表现出肌球蛋白相关调控；这些肌肉中有9块单独表现出这种调节形式。在存在或不存在MgATP的情况下，这些肌球蛋白在添加Ca2+时，Trp或Tyr荧光均未发生任何变化；在存在或不存在钙的情况下，所有肌球蛋白在添加MgATP时，Trp荧光变化很小或为零。因此，构象敏感的色氨酸，如兔肌球蛋白中存在的色氨酸，不是肌球蛋白atp酶的必要条件。用含氟基团的a -碘乙酰- a "-（l-磺基-5-萘基）乙二胺修饰若干光链，并将修饰后的光链加回0 -c去敏扇贝肌球蛋白中，观察荧光和荧光极化。在添加MgATP和/或钙后，这些pa参数没有变化。扇贝肌球蛋白和脱蛋白的圆二色光谱
Myosin was isolated from 14 invertebrate muscles all of which exhibited myosin-linked regulation; 9 of these muscles solely exhibited this form of regulation. None of these myosins showed any change in Trp or Tyr fluorescence upon addition of Ca2+ in the presence or absence of MgATP and all myosins showed either a small or zero Trp fluorescence change upon addition of MgATP in the presence or absence of calci-um. Thus a conformationally sensitive Trp, such as that present in rabbit myosin, is not a necessary requirement for the myosin ATPase. Several light chains were modified with the fluoro-phore A-iodoacetyl-A"-(l-sulfo-5-naphthyl) ethylenediamine and each modified light chain was added back to0 C-de-sensitized scallop myosin, and the fluorescence and fluores-cence polarization were examined. No change in these pa-rameters occurred upon addition of MgATP and/or calcium. Circular dichroism (CD) spectra of scallop myosin and de-