Behavior of uridine phosphorylase from Escherichia coli K-12 in hydrated reversed micelles of surfactant in organic solvent.
The catalytic activity of uridine phosphorylase from Escherichia coli K-12 entrapped in hydrated reversed micelles of aerosol OT (AOT) in octane has been studied as a function of the degree of hydration of micelles. It was shown that the catalytic activity reaches maximum values at ratios [H2O]/[AOT] equal to 8.4, 12.8, 16.1, and 18.6. On the basis of sedimentation data the conclusion has been made that the maximums of the catalytic activity of uridine phosphorylase correspond to monomeric, dimeric, trimeric, and tetrameric forms of the enzyme.
Kurganov
B I
BI
A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Burlakova
A A
AA
Chebotareva
N A
NA
Debabov
V G
VG
D001426:Bacterial Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D008823:Micelles; D009795:Octanes / Q000737:chemistry*; D012997:Solvents; D013501:Surface-Active Agents / Q000737:chemistry / Q000378:metabolism*; D014498:Uracil / Q000378:metabolism; D014529:Uridine / Q000378:metabolism; D014543:Uridine Phosphorylase / Q000378:metabolism*; D014867:Water / Q000737:chemistry
D001426:Bacterial Proteins; D008823:Micelles; D009795:Octanes; D012997:Solvents; D013501:Surface-Active Agents; D014867:Water; D014498:Uracil; D014543:Uridine Phosphorylase; D014529:Uridine; C026728:octane