THE BINDING OF CALCIUM TO HUMAN FIBRONECTIN
THE BINDING OF CALCIUM TO HUMAN FIBRONECTIN
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DOI：
10.1016/0006-291x(83)91405-5
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发表时间：
1983-01-01
影响因子：
3.1
通讯作者：
HRINDA, ME
中科院分区：
文献类型：
--
作者：
AMPHLETT, GW;HRINDA, ME
Ca2+与人血浆纤连蛋白的结合通过25°C的平衡透析来测量。 C 溶于 0.1 M NaCl 50 mM Tris HCL，pH 7.4。结合数据的曲线拟合表明纤连蛋白每条链有 2 个强 Ca 结合位点 (MW 220,000)，Kd = 1.3 mM 和.apprx。 12 个弱位点，Kd = 2.3 mM。当 Mg 浓度高达 1 mM 时，未观察到结合的 Fe 被 Mg 明显置换。研究了 Ca 与一对纤连蛋白胰蛋白酶片段（MW 160,000 和 180,000）的结合，该片段与明胶结合。这些片段具有单一类别的 Ca 结合位点，每条链有 2.2 个位点，Kd = 1.1 mM。观察到与来自纤连蛋白分子其他区域的胰蛋白酶片段的结合可以忽略不计。
The binding of Ca to human plasma fibronectin was measured by equilibrium dialysis at 25.degree. C in 0.1 M NaCl 50 mM Tris HCL, pH 7.4. Curve fitting of the binding data indicates that fibronectin has 2 strong Ca binding sites per chain (MW 220,000), Kd = 1.3 mM and .apprx. 12 weak sites, Kd = 2.3 mM. No significant displacement of bound Fe by Mg was observed at Mg concentrations up to 1 mM. Ca binding to a pair of tryptic fragments of fibronectin (MW .simeq. 160,000 and 180,000) that bind to gelatin was investigated. These fragments have a single class of Ca binding sites, with 2.2 sites per chain, Kd = 1.1 mM. Negligible Ca binding to tryptic fragments derived from other regions of the fibronectin molecule was observed.