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绵羊红细胞血影蛋白的自我缔合。

The self-association of ovine erythrocyte spectrin.

作者信息

Cole N, Ralston G B

机构信息

Department of Biochemistry, University of Sydney, NSW, Australia.

出版信息

Int J Biochem. 1993 Nov;25(11):1555-9. doi: 10.1016/0020-711x(93)90511-c.

Abstract
  1. Spectrin extracted from ovine erythrocyte membranes at low temperature shows association behaviour similar to that reported for human and bovine erythrocytes. 2. The spectrin tetramer is the predominant oligomer, the dimer is well represented, and smaller amounts of hexamer and higher oligomers are present. 3. The estimates of parameters describing the self-association of purified ovine spectrin studied by sedimentation equilibrium analysis were found to be indistinguishable from those obtained for human spectrin under the same conditions, within the precision of the measurements. 4. The data suggest that the cooperative isodesmic model may be general for spectrin, and not a peculiarity of the human.
摘要
  1. 低温下从绵羊红细胞膜中提取的血影蛋白表现出与人类和牛红细胞所报道的缔合行为相似。2. 血影蛋白四聚体是主要的寡聚体,二聚体也大量存在,还有少量六聚体和更高阶的寡聚体。3. 在测量精度范围内,通过沉降平衡分析研究的纯化绵羊血影蛋白自缔合参数估计值与相同条件下人类血影蛋白的估计值没有区别。4. 数据表明协同等键模型可能对血影蛋白具有普遍性,并非人类血影蛋白所特有。

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