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Phospholipid Transfer Proteins as Probes of Membrane Structure and Function

  • Chapter
Subcellular Biochemistry

Part of the book series: Subcellular Biochemistry ((SCBI,volume 16))

Abstract

The spontaneous redistribution of phospholipid between classes of unilamellar vesicles (Kornberg and McConnell, 1971; Ehnholm and Zilversmit, 1972) or between microsomal vesicles and mitochondria (Wirtz and Zilversmit, 1968) is very slow for most phospholipids (reviewed by Sleight, 1987; Dawidowicz, 1987a). Wirtz and Zilversmit (1968) and McMurray and Dawson (1969) demonstrated that phospholipid movement was stimulated by rat liver cytosol and later showed that proteins were responsible for this activity (reviewed by Wirtz, 1982). Lipid transfer proteins with various specificities and physical characteristics have now been purified from a number of biological sources, including animal tissues and plasma, plants, yeasts, and bacteria (see Section 2.1).

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Abbreviations

PC:

phosphatidylcholine

PE:

phosphatidyl ethanolamine

PI:

phosphatidylinositol

PS:

phosphatidylserine

PG:

phosphatidylglycerol

PA:

phosphatidic acid.

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  1. Department of Molecular and Cell Biology, The University of Connecticut, Storrs, Connecticut, 06268, USA

    Richard C. Crain

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  1. RUCA-Laboratory for Human Biochemistry, University of Antwerp, B2020, Antwerp, Belgium

    H. J. Hilderson

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Crain, R.C. (1990). Phospholipid Transfer Proteins as Probes of Membrane Structure and Function. In: Hilderson, H.J. (eds) Subcellular Biochemistry. Subcellular Biochemistry, vol 16. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1621-1_3

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  • DOI: https://doi.org/10.1007/978-1-4899-1621-1_3

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