Selective delipidation of the plasma membrane by surfactants : enrichment of sterols and activation of ATPase.

Abstract:

:The influence of plasma membrane lipid components on the activity of the H(+)-ATPase has been studied by determining the effect of surfactants on membrane lipids and ATPase activity of oat (Avena sativa L.) root plasma membrane vesicles purified by a two-phase partitioning procedure. Triton X-100, at 25 to 1 (weight/weight) Triton to plasma membrane protein, an amount that causes maximal activation of the ATPase in the ATPase assay, extracted 59% of the membrane protein but did not solubilize the bulk of the ATPase. The Triton-insoluble proteins had associated with them, on a micromole per milligram protein basis, only 14% as much phospholipid, but 38% of the glycolipids and sterols, as compared with the native membranes. The Triton insoluble ATPase could still be activated by Triton X-100. When solubilized by lysolecithin, there were still sterols associated with the ATPase fraction. Free sterols were found associated with the ATPase in the same relative proportions, whether treated with surfactants or not. We suggest that surfactants activate the ATPase by altering the hydrophobic environment around the enzyme. We propose that sterols, through their interaction with the ATPase, may be essential for ATPase activity.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Sandstrom RP,Cleland RE

doi

10.1104/pp.90.4.1524

subject

Has Abstract

pub_date

1989-08-01 00:00:00

pages

1524-31

issue

4

eissn

0032-0889

issn

1532-2548

journal_volume

90

pub_type

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