On the binding of dolichol by bovine liver supernatant.

摘要: Abstract Experimental evidence is presented that a bovine liver pH 5.1 supernatant possesses binding capacity towards dolichol. Optimal found at physiological and 5°C. At higher temperature the drastically reduced. After binding, labelled ligand cannot be chased by unlabelled Scatchard analysis indicates single class of sites ( B max = 3.6 pmol/mg protein) with an apparent K d 1.8 · 10 −11 M. Only dolichol dolichyl derivatives reduce phenomenon. The involvement protein-like structure inferred from ammonium sulphate precipitation proteolysis experiments. Exclusion chromatography gel electrophoresis under nondenaturating conditions indicate high molecular weight complex. Upon SDS electrophoresis, bound [ 3 H]dolichol comigrates protein band M r ≈ 25000).