Nature of the Elements Transporting Long-Chain Fatty Acids Through the Red Cell Membrane

Nature of the Elements Transporting Long-Chain Fatty Acids Through the Red Cell Membrane Docosahexaenoic acid is found to be bound to three equivalent sites on albumin with the same affinities as palmitic acid at 0–38°C, which demonstrates that ethene-1,2-diyl- and methylene-groups contribute equally to the affinity. The equilibrium dissociation constants (K dm s) for red cell membrane binding sites of linoleic- and docosahexaenoic acid at pH 7.3 are determined at temperatures between 0 and 37°C. The temperature-independent capacities for binding are 12 ± 1 and 25.4 ± 3.0 nmoles g−1 ghosts respectively. Double isotope binding experiments reveal that the unsaturated fatty acids: arachidonic-, linoleic-, docosahexaenoic-, and oleic acid have partially shared capacities in ratios approximately 1:2:4:5, in contrast to the noncompetitive binding of palmitic acid. The observations suggest a two-tier binding limitation. One is the number of protein sites binding fatty acid anions electrostatically and the other is the number of suitable annular lipids adaptively selected among membrane lipids by the hydrocarbon chain. These competition conditions are confirmed by measurements of the tracer exchange efflux at near 0°C from albumin-free and albumin-filled ghosts of linoleic- and docosahexaenoic acid, either alone or in the presence of arachidonic- and palmitic acid. Under equilibrium conditions, the calculated ratios of inside to outside membrane binding is below 0.5 for four unsaturated fatty acids. The unidirectional rate constants of translocation between the inside and the outside correlate with the number of double bonds in these fatty acids, which are also correlated with the dissociation rate constants of the complexes with albumin. The membrane permeation occurs presumably by binding of the anionic unsaturated fatty acids to an integral protein followed by channeling of the neutral form between opposite binding sites of the protein through annular lipids encircling the protein. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Nature of the Elements Transporting Long-Chain Fatty Acids Through the Red Cell Membrane

Loading next page...
 
/lp/springer_journal/nature-of-the-elements-transporting-long-chain-fatty-acids-through-the-fh5bcA2suK
Publisher
Springer-Verlag
Copyright
Copyright © Inc. by 1998 Springer-Verlag New York
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s002329900381
Publisher site
See Article on Publisher Site

Abstract

Docosahexaenoic acid is found to be bound to three equivalent sites on albumin with the same affinities as palmitic acid at 0–38°C, which demonstrates that ethene-1,2-diyl- and methylene-groups contribute equally to the affinity. The equilibrium dissociation constants (K dm s) for red cell membrane binding sites of linoleic- and docosahexaenoic acid at pH 7.3 are determined at temperatures between 0 and 37°C. The temperature-independent capacities for binding are 12 ± 1 and 25.4 ± 3.0 nmoles g−1 ghosts respectively. Double isotope binding experiments reveal that the unsaturated fatty acids: arachidonic-, linoleic-, docosahexaenoic-, and oleic acid have partially shared capacities in ratios approximately 1:2:4:5, in contrast to the noncompetitive binding of palmitic acid. The observations suggest a two-tier binding limitation. One is the number of protein sites binding fatty acid anions electrostatically and the other is the number of suitable annular lipids adaptively selected among membrane lipids by the hydrocarbon chain. These competition conditions are confirmed by measurements of the tracer exchange efflux at near 0°C from albumin-free and albumin-filled ghosts of linoleic- and docosahexaenoic acid, either alone or in the presence of arachidonic- and palmitic acid. Under equilibrium conditions, the calculated ratios of inside to outside membrane binding is below 0.5 for four unsaturated fatty acids. The unidirectional rate constants of translocation between the inside and the outside correlate with the number of double bonds in these fatty acids, which are also correlated with the dissociation rate constants of the complexes with albumin. The membrane permeation occurs presumably by binding of the anionic unsaturated fatty acids to an integral protein followed by channeling of the neutral form between opposite binding sites of the protein through annular lipids encircling the protein.

Journal

The Journal of Membrane BiologySpringer Journals

Published: Jun 1, 1998

There are no references for this article.

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off