Crimmins D L, Holtzer M E
Howard Hughes Medical Institute Core Protein/Peptide Facility, Washington University School of Medicine, St. Louis, MO 63110.
J Chromatogr. 1991 May 10;543(2):327-43. doi: 10.1016/s0021-9673(01)95785-1.
Non-cross-linked and disulfide-cross-linked two-chain molecules comprising the alpha and/or beta chains of rabbit skeletal tropomyosin were studied by electrophoretic, chromatographic and physical methods. Elution order on C4 reversed-phase high-performance liquid chromatography depends markedly on the number and position of the cross-links. In the C4 reversed-phase elution medium, cross-linked and non-cross-linked species are greater than 85% helical by circular dichroism, but the non-cross-linked elute later from high-performance size-exclusion chromatography (G4000) and have molecular mass of 31,000-41,000 dalton by equilibrium ultracentrifugation. The data suggest that in the C4 reversed-phase high-performance liquid chromatography elution medium non-cross-linked tropomyosin exists as amphipathic single-chain alpha-helices.
通过电泳、色谱和物理方法研究了包含兔骨骼肌原肌球蛋白α链和/或β链的非交联和二硫键交联的双链分子。在C4反相高效液相色谱上的洗脱顺序明显取决于交联的数量和位置。在C4反相洗脱介质中，通过圆二色性分析，交联和非交联的物种螺旋度均大于85%，但非交联的物种在高效尺寸排阻色谱（G4000）中洗脱较晚，并且通过平衡超速离心法测得其分子量为31,000 - 41,000道尔顿。数据表明，在C4反相高效液相色谱洗脱介质中，非交联的原肌球蛋白以两亲性单链α螺旋形式存在。
