24 June 1988 Quantitative Characterization Of The Interactions Of Some Glycolytic Enzymes: An Application Of The Fluorescence Anisotropy Measurement
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Proceedings Volume 0909, Time-Resolved Laser Spectroscopy in Biochemistry; (1988) https://doi.org/10.1117/12.945379
Event: 1988 Los Angeles Symposium: O-E/LASE '88, 1988, Los Angeles, CA, United States
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.
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Peter Tompa, Jorg Bar, Jozsef Batke, "Quantitative Characterization Of The Interactions Of Some Glycolytic Enzymes: An Application Of The Fluorescence Anisotropy Measurement", Proc. SPIE 0909, Time-Resolved Laser Spectroscopy in Biochemistry, (24 June 1988); doi: 10.1117/12.945379; https://doi.org/10.1117/12.945379
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