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原肌球蛋白与肌钙蛋白各组分的相互作用。

Interaction of tropomyosin with troponin components.

作者信息

Dabrowska R, Podlubnaya Z, Nowak E, Drabikowski W

出版信息

J Biochem. 1976 Jul;80(1):89-99. doi: 10.1093/oxfordjournals.jbchem.a131262.

Abstract
  1. The TN-T and TN-I components of troponin both interact with tropomyosin and cause its precipitation in 0.1 M KC1 at neutral pH. The precipitate contains both end-to-end and side-by-side aggregates of tropomyosin molecules. 2. The TN-T and TN-I components change the band pattern of tropomyosin paracrystals formed in MgC1(2) solutions, although in different ways. TN-T causes the formation of hexagonal net structures, double-stranded net or paracrystals which result from the collapse of the double-stranded net. TN-I at pH 7.9 causes the formation of paracrystals with a 400 A periodic band pattern and a 200 A repeat. The same band pattern can also be seen in tropomyosin paracrystals formed at pH values below 6.0. 3. The TN-C component does not precipitate tropomyosin in 0.1 M KC1. The aggregates of tropomyosin obtained with either TN-T or TN-I can be solubilized by the addition of TN-C. No interaction of TN-C was observed with tropomyosin paracrystals formed in the presence of MgC12.
摘要
  1. 肌钙蛋白的TN-T和TN-I组分均与原肌球蛋白相互作用,并在中性pH值的0.1 M KCl中使其沉淀。沉淀物包含原肌球蛋白分子的端对端和并排聚集体。2. TN-T和TN-I组分以不同方式改变在MgCl₂溶液中形成的原肌球蛋白副晶体的条带模式。TN-T导致形成六边形网状结构、双链网或由双链网塌陷产生的副晶体。pH 7.9时的TN-I导致形成具有400 Å周期性条带模式和200 Å重复的副晶体。在pH值低于6.0时形成的原肌球蛋白副晶体中也可以看到相同的条带模式。3. TN-C组分在0.1 M KCl中不会使原肌球蛋白沉淀。用TN-T或TN-I获得的原肌球蛋白聚集体可通过添加TN-C而溶解。未观察到TN-C与在MgCl₂存在下形成的原肌球蛋白副晶体有相互作用。

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