Binding of Adenosine 5'-Monophosphate to Bovine Liver Fructose 1,6-Bisphosphatase

1 July 1979

journal article
research article
Published by S. Karger AG in Enzyme

Vol. 24 (2) , 132-136
https://doi.org/10.1159/000458641

Abstract

Bovine liver fructose 1,6-bisphosphatase bound 4 mol of its allosteric inhibitor AMP per mole of enzyme with half-saturation at 17 jumol/1 AMP. The presence of a mixture of positive and negative cooperativity in the binding of AMP to the enzyme was suggested by several procedures for analyzing binding data. In particular, calculation of the intrinsic binding constants for AMP yielded the relationships: K(1)' K(3)' <K(4)', indicating mixed cooperativity.

Keywords

FRUCTOSE 1
6-BISPHOSPHATASE
NEGATIVE COOPERATIVITY
ALLOSTERISM

This publication has 2 references indexed in Scilit:

DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*
Annals of the New York Academy of Sciences, 1964
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Journal of Biological Chemistry, 1951