PMID: 6404625Apr 5, 1983Paper

Effect of sodium cholate on the catalytic and structural properties of phosphorylase b

European Journal of Biochemistry
T G SotiroudisA E Evangelopoulos

Abstract

Sodium cholate at millimolar concentration is able to induce activity in rabbit muscle phosphorylase b in the absence of AMP. The maximum activation of the enzyme in presence of 7 mM sodium cholate was 24% of that achieved by 1 mM AMP. Other bile salts tested showed a negligible activating effect. The Ka for AMP was lowered fivefold by 5 mM of the steroid detergent, while the cooperative binding of the nucleotide was abolished. Phosphorylase b', a modified form of phosphorylase in which the phosphorylation site has been removed by limited tryptic attack, presented an activation profile similar to that of phosphorylase b. In contrast, phosphorylase a was inhibited by the bile salt, while the activity of liver phosphorylase b was not significantly affected. Modification of the AMP site of the enzyme with 2,3-butanedione could not inhibit sodium-cholate-induced activity. tert-Butanol, an organic solvent activator of phosphorylase b, was found to enhance the activity induced by sodium cholate. The interaction of sodium cholate and phosphorylase b was also followed by difference spectroscopy using a fluorescein isothiocyanate--phosphorylase b conjugate. Furthermore, measurements of electron spin resonance demonstrated that the mobil...Continue Reading

References

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Citations

Dec 1, 1992·Journal of Bioenergetics and Biomembranes·F CentenoC Gutierrez-Merino
Jan 1, 1996·The International Journal of Biochemistry & Cell Biology·A M Psarra, T G Sotiroudis
Jun 20, 2001·Clinica Chimica Acta; International Journal of Clinical Chemistry·C D KarapittaT G Sotiroudis
Sep 16, 1985·European Journal of Biochemistry·S Nikolaropoulos, T G Sotiroudis
Jun 5, 1986·Biochimica Et Biophysica Acta·S M KyriakidisA E Evangelopoulos
Dec 20, 1985·Biochimica Et Biophysica Acta·N G OikonomakosL N Johnson

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