[Effect of hydrostatic pressure on quaternary structure on the chaperone function of alpha-crystallin].
High hydrostatic pressure-induced changes in bovine lens alpha-crystallin oligomers size and chaperone-like function were studied by a static light scattering. Under pressure 1.5 kbar, alpha-crystallin oligomers size is almost unaffected. Increase of the size was observed during several hours of incubation at 3 kbar. Such high-pressure effect on association has been previously revealed for detergent micelles, whereas the "typical" protein oligomers are known to dissociate under high pressure. Our results about pressure influence on alpha-crystallin association supports the previously proposed "protein micelle" model of the protein quaternary structure. Chaperone-like activity of alpha-crystallin is shown to increase after incubation at 3 kbar. After the end of the incubation this activity is slowly decreasing during several hours.
Avilov
S
S
Palladin Institute of Biochemistry of NAS of Ukraine, Kyiv.
Bode
Ch
Ch
Told'oshr
F
F
Demchenko
O
O
D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000737:chemistry / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D008823:Micelles; D018832:Molecular Chaperones / Q000737:chemistry / Q000502:physiology*; D011312:Pressure; D020836:Protein Structure, Quaternary
D003459:Crystallins; D008823:Micelles; D018832:Molecular Chaperones