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Behavior of uridine phosphorylase from Escherichia coli K‐12 in hydrated reversed micelles of surfactant in organic solvent

Behavior of uridine phosphorylase from Escherichia coli K‐12 in hydrated reversed micelles of... 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 (H20)/(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 monomenc, dimeric, trimeric, and tetrameric forms of the enzyme. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png IUBMB Life Wiley

Behavior of uridine phosphorylase from Escherichia coli K‐12 in hydrated reversed micelles of surfactant in organic solvent

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References (1)

Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
Copyright © 1997 International Union of Biochemistry and Molecular Biology
ISSN
1521-6543
eISSN
1521-6551
DOI
10.1080/15216549700201571
Publisher site
See Article on Publisher Site

Abstract

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 (H20)/(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 monomenc, dimeric, trimeric, and tetrameric forms of the enzyme.

Journal

IUBMB LifeWiley

Published: Mar 1, 1997

Keywords: Uridine phosphorylase; catalytic activity of oligomeric lbrms; hydrated reversed micelles; sedimentation

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