Sedimentation analysis of muscle glycogen phosphorylase b entrapped in hydrated reversed micelles of aerosol OT in octane.
The oligomeric state and formation of supramolecular structures of glycogen phosphorylase b from rabbit skeletal muscles have been studied in the system of hydrated reversed micelles of aerosol OT (AOT) in octane. Sedimentation studies show that the oligomeric state of the enzyme is controlled by the degree of hydration of micelles. Monomeric, dimeric, trimeric, tetrameric, hexameric, or octameric forms of the enzyme were observed depending on the degree of micelle hydration.
Kurganov
B I
BI
A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Chebotareva
N A
NA
D000818:Animals; D004143:Dioctyl Sulfosuccinic Acid; D004339:Drug Compounding; D046911:Macromolecular Substances; D008823:Micelles; D018482:Muscle, Skeletal / Q000201:enzymology*; D009795:Octanes; D010763:Phosphorylase b / Q000737:chemistry*; D011487:Protein Conformation; D011817:Rabbits; D014461:Ultracentrifugation; D014867:Water / Q000378:metabolism
D046911:Macromolecular Substances; D008823:Micelles; D009795:Octanes; D014867:Water; D004143:Dioctyl Sulfosuccinic Acid; D010763:Phosphorylase b; C026728:octane