van Dessel G, de Wolf M, Lagrou A, Hilderson H J, Dierick W
Biochim Biophys Acta. 1986 Oct 3;878(3):346-52. doi: 10.1016/0005-2760(86)90242-0.
The presence of a dolichol binding system is demonstrated in human serum. The dolichol binding exhibits normal saturation kinetics with an apparent affinity constant Kd of 6.9 X 10(-6) M. Optimal binding is obtained at pH 7.4 and 5 degrees C. After binding the [3H]dolichol cannot be chased by unlabelled dolichol. The selectivity is examined by competition studies showing that only dolichyl derivatives equally compete for binding sites. From buoyant density centrifugation and gel filtration it is deduced that the dolichol binding is due to a serum protein fraction, displaying the characteristics of VLDL.
在人血清中证实存在多萜醇结合系统。多萜醇结合表现出正常的饱和动力学,表观亲和常数Kd为6.9×10⁻⁶ M。在pH 7.4和5℃条件下可获得最佳结合效果。结合后,未标记的多萜醇无法取代已结合的[³H]多萜醇。通过竞争研究检测选择性,结果表明只有多萜醇衍生物能同等程度地竞争结合位点。通过浮力密度离心和凝胶过滤推断,多萜醇结合是由一种血清蛋白组分引起的,该组分具有极低密度脂蛋白(VLDL)的特征。