PMID: 3756199Oct 3, 1986Paper

On the binding of dolichol by human serum

Biochimica Et Biophysica Acta
G van DesselW Dierick

Abstract

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.

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Citations

Dec 22, 1999·Journal of Hepatology·K HumalojaM Salaspuro
Oct 3, 1986·Biochimica Et Biophysica Acta·G van DesselW Dierick
Jun 1, 1994·Metabolism: Clinical and Experimental·M MarinoA Trentalance
Jun 17, 1999·Annals of Clinical Biochemistry·M KuriyamaM Osame

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