Rotational relaxation of free and protease-bound alpha2-macroglobulin.
Rotational relaxation of free and protease-bound alpha2-macroglobulin.
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发表时间：
1978-10
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通讯作者：
F. Pochon;B. Amand;D. Lavalette;J. Bieth
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作者：
F. Pochon;B. Amand;D. Lavalette;J. Bieth
最近描述的三重探针去极化技术已被用来研究自由和蛋白酶结合的α 2-巨球蛋白的旋转弛豫。发现游离球蛋白的分子斯托克斯半径为88 A，当与干燥半径相比时，该值表明高度水合。α 2-巨球蛋白与糜蛋白酶结合后的相关时间没有变化，但在纤溶酶存在下略有增加。在存在4 M尿素的情况下，α 2-巨球蛋白解离成亚基，这种解离不会导致结合蛋白酶的释放。
The recently described triplet probe depolarization technique has been utilized to investigated the rotational relaxation of free and protease-bound alpha2-macroglobulin. The molecular Stokes radius of the free globulin was found to be 88 A, a value which, when compared to the dry radius, indicates a high degree of hydration. The correlation time of alpha2-macroglobulin does not change after its binding with chymotrypsin, but slightly increases in the presence of plasmin. In the presence of 4 M urea, alpha2-macroglobulin dissociates into subunits and this dissociation does not lead to a release of the bound proteases.