The somatomedin C binding protein: evidence for a heterologous subunit structure.
The somatomedin C binding protein: evidence for a heterologous subunit structure.
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生长调节素 C 结合蛋白：异源亚基结构的证据。
DOI：
10.1210/jcem-51-1-12
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发表时间：
1980
期刊：
影响因子：
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通讯作者：
Richard W. Furlanetto
中科院分区：
文献类型：
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作者：
Richard W. Furlanetto
用Sephadex G-200柱层析，在pH 7.40条件下，研究了生长抑素C与血清蛋白的结合。在此条件下，全血中免疫活性生长抑素C的斯托克斯半径为43A(Kd=0.25)。经硫酸铵沉淀和DEAE Sephadex柱层析，得到三个蛋白质峰。第二个峰含有大部分免疫反应阳性的生长激素C，但这一组分中的生长激素的斯托克斯半径分别为36和14A(Kd分别为0.35和0.75)。该组分与DEAE Sephadex峰3组分的重组导致了43A(Kd=0.25)物种的重现。用Sephadex G-50在0.1M冰醋酸-0.15M氯化钠溶液中对43A生长抑素C组分进行层析，使生长抑素C从其结合蛋白中分离出来。结合蛋白在G-50柱的空隙体积分数中被回收。这种酸处理的结合蛋白的斯托克斯半径为36A(Kd=0.35)，由[125I]生长抑素C在pH 7.40时的结合测定。当..。
The binding of somatomedin C to serum proteins was investigated using Sephadex G-200 chromatography at pH 7.40. Under these conditions, immunoreactive somatomedin C in whole serum has a Stokes' radius of 43 A (Kd = 0.25). After ammonium sulfate precipitation and DEAE Sephadex chromatography, three protein peaks were obtained. The second peak contained the majority of the immunoreactive somatomedin C, but the somatomedin in this fraction has Stokes' radii of 36 and 14 A (Kd = 0.35 and 0.75, respectively). Recombining this fraction with the DEAE Sephadex peak 3 fraction resulted in the reappearance of the 43 A (Kd = 0.25) species. Chromatography of the 43 A somatomedin C species on Sephadex G-50 in 0.1 M acetic acid-0.15 M NaCl dissociated somatomedin C from its binding protein. The binding protein was recovered in the void volume fractions of the G-50 column. This acid-treated binding protein had a Stokes' radius of 36 A (Kd = 0.35), as determined by the binding of [l25I]somatomedin C at pH 7.40. When the ...