Grunau C, Dettmer R, Behlke J, Bernhardt R
Max-Delbrück-Centrum für Molekulare Medizin, Berlin-Buch, Germany.
Biochem Biophys Res Commun. 1995 May 25;210(3):1001-8. doi: 10.1006/bbrc.1995.1756.
The interaction of bovine adrenodoxin with the chaperonin GroEL was investigated using sucrose density centrifugation and analytical ultracentrifugation. It could be clearly established that denatured mature adrenodoxin comigrated in a sucrose density gradient with the GroEL oligomer, indicating that a complex had been formed. Up to 2 moles of adrenodoxin/mol GroEL can be bound. From the partial concentrations, association constants of 4.3 x 10(5) M-1 for the first adrenodoxin molecule and of 1.08 x 10(5) M-1 for the second molecule to the complex, respectively, were calculated. Upon addition of the cochaperonin GroES and Mg-ATP to the adrenodoxin-GroEL complex, adrenodoxin was released, indicating a specific binding between GroEL and adrenodoxin.
利用蔗糖密度离心法和分析超速离心法研究了牛肾上腺皮质铁氧化还原蛋白与伴侣蛋白GroEL的相互作用。可以明确证实，变性的成熟肾上腺皮质铁氧化还原蛋白在蔗糖密度梯度中与GroEL寡聚体一起迁移，这表明已经形成了复合物。每摩尔GroEL最多可结合2摩尔肾上腺皮质铁氧化还原蛋白。根据部分浓度，分别计算出第一个肾上腺皮质铁氧化还原蛋白分子与复合物的缔合常数为4.3×10⁵ M⁻¹，第二个分子与复合物的缔合常数为1.08×10⁵ M⁻¹。向肾上腺皮质铁氧化还原蛋白-GroEL复合物中加入共伴侣蛋白GroES和Mg-ATP后，肾上腺皮质铁氧化还原蛋白被释放，这表明GroEL与肾上腺皮质铁氧化还原蛋白之间存在特异性结合。
