[Regulation of supermolecular organization and catalytic activity of the lysosomal complex GM1-galactosidase and neuraminidase in vitro].
The regulation of the catalytic activity and supramolecular organization of human kidney Gm1-galactosidase and neuraminidase was investigated in the reversed micellar systems of Aerosol OT in octane. It was found that in the reversed micellar systems the Gm1-galactosidase can exist in the monomeric, tetrameric or octameric forms depending on the H2O/surfactant ratio in the system which determines the micelle size. The association of Gm1-galactosidase monomers into octameric structure characteristic of Gm1-galactosidase in the lysosomes results in a two fold increase of the specific catalytic activity of the enzyme. 32 kDa "protective" protein--the component of Gm1-galactosidase--neuraminidase native complex was found to improve significantly this association.
Pshezhetskiĭ
A V
AV
Levashov
A V
AV
Vidershaĭn
G Ia
GIa
D002384:Catalysis; D004796:Clinical Enzyme Tests; D006801:Humans; D007668:Kidney / Q000201:enzymology; D008823:Micelles; D009097:Multienzyme Complexes / Q000378:metabolism; D009439:Neuraminidase / Q000378:metabolism*; D001616:beta-Galactosidase / Q000378:metabolism*
D008823:Micelles; D009097:Multienzyme Complexes; D009439:Neuraminidase; C021502:acid beta-galactosidase; D001616:beta-Galactosidase
Reguliatsiia nadmolekuliarnoĭ organizatsii i kataliticheskoĭ aktivnosti lizosomnogo kompleksa GM!-galaktozidazy i neĭraminidazy in vitro.