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(Received for publication, April 16, 1997, and in revised form, May 20, 1997)
From the Lipopolysaccharide (LPS)-binding protein (LBP)
and bactericidal/permeability-increasing protein (BPI) are closely
related LPS-binding proteins whose binding to LPS has markedly
different functional consequences. To gain better insight into the
possible basis of these functional differences, the physical properties of LBP-LPS and BPI-LPS complexes have been compared in this study by
sedimentation, light scattering, and fluorescence analyses. These
studies reveal dramatic differences in the physical properties of LPS
complexed to LBP versus BPI. They suggest that of the two proteins, only LBP can disperse LPS aggegates. However, BPI can enhance
both the sedimentation velocity and apparent size of LPS aggregates
while inhibiting LPS-LBP binding even at very low (1:40 to 1:20)
BPI:LPS molar ratios.
Volume 272, Number 30,
Issue of July 25, 1997
pp. 18682-18685
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
and Department of Immunology, The Scripps
Research Institute, La Jolla, California 92037 and the Departments
of Medicine and ¶ Microbiology, New York University School
of Medicine, New York, New York 10016
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