Sedimentation velocity analysis of oligomeric enzymes in hydrated reversed micelles of surfactants in organic solvents View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1999-09-20

AUTHORS

N. A. Chebotareva , B. I. Kurganov , A. A. Burlakova

ABSTRACT

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 sodium bis-2-ethylhexyl sulfosuccinate (aerosol OT, AOT) in octane. Sedimentation analysis shows that the oligomeric state of the enzyme is controlled by the degree of hydration of the micelles ([H2O]/ [AOT] = w0). The monomeric (in the range of w0 from 10 to 16), dimeric (10 < w0 < 30), trimeric (30 < w0 < 38), tetrameric (23 < w0 < 42), hexameric (41 < w0 < 50), or octameric forms (48 < w0 < 53) of the enzyme were observed depending on the degree of hydration. Sedimentation behaviour of uridine phosphorylase from Esc-herichia coli K-12 in the micellar system was studied in the range of w0 from 8.4 to 23.9. The monomeric (at w0 = 8.4), dimeric (at w0 = 12.9), trimeric (at w0 = 16.1), tetrameric (at w0 = 18.6) and hexameric (at w0 = 23.9) enzyme forms were registered. The results obtained show that the hydrated reversed micelles are a powerful tool for the study of not only dissociated forms of oligomeric enzymes but also supra-molecular structures. These latter structures mimic the ordered supramolecular complexes of the enzymes whose formation is favoured by the crowded molecular conditions encountered in vivo. More... »

PAGES

129-134

References to SciGraph publications

Book

TITLE

Analytical Ultracentrifugation V

ISBN

978-3-540-66175-7

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/3-540-48703-4_18

DOI

http://dx.doi.org/10.1007/3-540-48703-4_18

DIMENSIONS

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