[Effect of the method of extracting the pore-forming protein from Yersinia pseudotuberculosis on its macromolecular organization].
By means of physico-chemical methods, lipid bilayer reconstitution and immunoenzyme assay, macromolecular organization of porin oligomers from Yersinia pseudotuberculosis, isolated by two extraction methods, was studied. Use of SDS and high temperature in the course of the extraction led to a partial denaturation of porin trimers at the level of the tertiary structure, these conformational changes affecting the porin's pore-forming activity and antigenic structure. At the same time, the partially denatured trimers are as stable under the treatment of urea and guanidine hydrochloride as the native protein.
Novikov
O D
OD
Fedoreeva
L I
LI
Khomenko
V A
VA
Portniagina
O Iu
OIu
Ermak
I M
IM
Likhatskaia
G N
GN
Moroz
S V
SV
Solov'eva
T F
TF
Ovodov
Iu S
IuS
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D007124:Immunoenzyme Techniques; D007473:Ion Channels; D008051:Lipid Bilayers; D018272:Porins; D011487:Protein Conformation; D011489:Protein Denaturation; D015011:Yersinia pseudotuberculosis / Q000737:chemistry*
D001425:Bacterial Outer Membrane Proteins; D007473:Ion Channels; D008051:Lipid Bilayers; D018272:Porins