[Interaction of the outer membrane pore-forming protein of Yersinia pseudotuberculosis with lipid A and its synthetic analogs].
Interaction of the major outer membrane protein form Yersinia pseudotuberculosis with lipid A was investigated by intrinsic fluorescence, CD spectroscopy and CsCl gradient centrifugation methods. The protein was shown to have two independent binding sites with an association constant 6.1 x 10(4) M-1. The interaction depends on both the type of the glycoside bond and hydrophilic--hydrophobic balance of the glycolipid molecule.
Fedoreeva
L I
LI
Gorbach
V I
VI
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D002942:Circular Dichroism; D008050:Lipid A / Q000031:analogs & derivatives / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D014461:Ultracentrifugation; D015011:Yersinia pseudotuberculosis / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D008050:Lipid A
Vzaĭmodeistvie poroobrazuiushchego belka vneshnei membrany Yersinia pseudotuberculosis s lipidom A i ego sinteticheskimi analogami.