Localization of the Potassium Ion Activation Site in Human Liver Fructose 1,6-Bisphosphatase

Three mouse monoclonal antibodies of human liver fructose 1,6-bisphosphatase are shown to bind to the enzyme at different sites as determined by ELISA. The binding of one of the monoclonal antibodies, L2E1, mimics the effects of K + ions, including increase in the enzyme activity and enhancement of...

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Veröffentlicht in:Biochemical and biophysical research communications 1993-08, Vol.194 (3), p.1483-1490
Hauptverfasser: Xu, G.J., Yu, Z.B., Hu, G.F., Cao, H.T.
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Sprache:eng
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Zusammenfassung:Three mouse monoclonal antibodies of human liver fructose 1,6-bisphosphatase are shown to bind to the enzyme at different sites as determined by ELISA. The binding of one of the monoclonal antibodies, L2E1, mimics the effects of K + ions, including increase in the enzyme activity and enhancement of the sensitivity of the enzyme to AMP inhibition. We tentatively suggest that human liver FruP 2ase may have a specific K + activation site, which at least partially overlaps with the L2E1 binding region. This site has been localized by analyzing the peptide fragments formed by cleavage with cyanogen bromide.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1993.1992