Intracellular trafficking of dolichol: on the presence of dolichol transfer activity in bovine liver supernatant.

G Van Dessel; A Lagrou

doi:10.18388/abp.1994_4720

Intracellular trafficking of dolichol: on the presence of dolichol transfer activity in bovine liver supernatant.

G Van Dessel UIA-Laboratory for Pathological Biochemistry, Belgium.;
A Lagrou

DOI: https://doi.org/10.18388/abp.1994_4720

Abstract

A protein catalyzing dolichol transfer between membranes has been purified from bovine liver up to 600-fold by acid precipitation, ammonium sulfate precipitation, ion-exchange chromatography and hydrophobic interaction chromatography. The protein displays a relative molecular mass of 15000 on SDS-gel electrophoresis. Kinetics as well as the influence of a series of effectors were studied. The transfer activity is inhibited by sphingomyelin, sulfhydryl groups and cationic amphiphilic amines with a bulky heterocyclic aromatic function. High salt concentration decreases the transfer efficiency. Transfer of dolichol between vesicles and mitochondria is not affected by the presence of moderate amounts of cholesterol in the donor vesicles. The overall characteristics of dolichol transfer activity are discussed in comparison to these of other lipid transfer proteins.

Published

1994-09-30

Issue

Vol. 41 No. 3 (1994)

Section

Articles

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