| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophys J, February 2001, p. 738-748, Vol. 80, No. 2
§ and
*National Institute of Bioscience and Human Technology, Tsukuba
305-8566, Japan; Instrumentation and Biophysics Branch,
Food and Drug Administration, Washington, DC 20204, and
National Biomedical EPR Center, Biophysics Research
Institute, Medical College of Wisconsin, Milwaukee WI 53226 USA;
§Biophysics Department, Institute of Molecular Biology,
Jagiellonian University, Krakow 31-120, Poland;
¶Department of Biological Science, Graduate School of
Science, Nagoya University, Nagoya 464-8602, and Kusumi
Membrane Organizer Project, Exploratory Research for Advancement of
Technology Organization, Japan Science and Technology Cooperation,
Nagoya 460-0012, Japan
A pulse saturation-recovery electron paramagnetic
resonance (EPR) method has been developed that allows estimation of the exchange rates of a spin-labeled lipid between the bulk domain and the
protein-rich membrane domain, in which the rate of collision between
the spin label and molecular oxygen is reduced (slow-oxygen transport
domain, or SLOT domain). It is based on the measurements of
saturation-recovery signals of a lipid spin label as a function of
concentrations of both molecular oxygen and the spin label. Influenza
viral membrane, one of the simplest paradigms for the study of
biomembranes, showed the presence of two membrane domains with slow and
fast collision rates with oxygen (a 16-fold difference) at 30°C. The
outbound rate from and the inbound rate into the SLOT domain (or
possibly the rate of the domain disintegration and formation) were
estimated to be 7.7 × 104 and 4.6 × 104 s
1, (15 µs residency time),
respectively, indicating that the SLOT domain is highly dynamic and
that the entire SLOT domain represents about one-third of the membrane
area. Because the oxygen transport rate in the SLOT domain is a factor
of two smaller than that in purple membrane, where bacteriorhodopsin is
aggregated, we propose that the SLOT domain in the viral membrane is
the cholesterol-rich raft domain stabilized by the trimers of
hemagglutinin and/or the tetramers of neuraminidase.
Biophys J, February 2001, p. 738-748, Vol. 80, No. 2
© 2001 by the Biophysical Society 0006-3495/01/02/738/11 $2.00
This article has been cited by other articles:
 |
|
 |
|
  W. K. Subczynski, A. Wisniewska, J. S. Hyde, and A. Kusumi Three-Dimensional Dynamic Structure of the Liquid-Ordered Domain in Lipid Membranes as Examined by Pulse-EPR Oxygen Probing Biophys. J., March 1, 2007; 92(5): 1573 - 1584. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Pyka, J. Ilnicki, C. Altenbach, W. L. Hubbell, and W. Froncisz Accessibility and Dynamics of Nitroxide Side Chains in T4 Lysozyme Measured by Saturation Recovery EPR Biophys. J., September 1, 2005; 89(3): 2059 - 2068. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. A. G. Briggs, T. Wilk, and S. D. Fuller Do lipid rafts mediate virus assembly and pseudotyping? J. Gen. Virol., April 1, 2003; 84(4): 757 - 768. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 U. Salzer, P. Hinterdorfer, U. Hunger, C. Borken, and R. Prohaska Ca++-dependent vesicle release from erythrocytes involves stomatin-specific lipid rafts, synexin (annexin VII), and sorcin Blood, April 1, 2002; 99(7): 2569 - 2577. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
