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Proceedings Paper

Quantitative Characterization Of The Interactions Of Some Glycolytic Enzymes: An Application Of The Fluorescence Anisotropy Measurement
Author(s): Peter Tompa; Jorg Bar; Jozsef Batke
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Paper Abstract

The affinity of Saccharomyces cerevisiae fructose-1,6-bisphosphate aldolase towards the metabolically related enzymes phosphofructokinase (PFK), triosephosphate isomerase (TPI) and glyceraldehyde-3-phosphate dehydrogenase (GPDH) was tested by using the signal of fluorescein isothiocyanate (FITC) attached covalently to the aldolase. The dissociation constants of the enzyme-enzyme complexes and rate constants of their formation and dissociation were measured and compared with the same parameters derived for enzymes from rabbit muscle. Hybrid complex formation between yeast aldolase and muscle GPDH and between muscle aldolase and yeast GPDH have also been observed. From the similarities in the determined parameters for the yeast and muscle enzymes we concluded that organization based on direct enzyme-enzyme interactions may be an ancient characteristic of the cytoplasm. The existence of in vitro hybrid complexes indicates that the recognition sites responsible for these interactions may have been conserved during the evolution.

Paper Details

Date Published: 24 June 1988
PDF: 3 pages
Proc. SPIE 0909, Time-Resolved Laser Spectroscopy in Biochemistry, (24 June 1988); doi: 10.1117/12.945379
Show Author Affiliations
Peter Tompa, Institute of Enzymology (Hungary)
Jorg Bar, Karl-Marx-University (Germany)
Jozsef Batke, Institute of Enzymology (Hungary)

Published in SPIE Proceedings Vol. 0909:
Time-Resolved Laser Spectroscopy in Biochemistry
Joseph R. Lakowicz, Editor(s)

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