Binding of adenosine 5'-monophosphate to bovine liver fructose 1,6-bisphosphatase

Bovine liver fructose 1,6-bisphosphatase bound 4 mol of its allosteric inhibitor AMP per mole of enzyme with half-saturation at 17 mumol/l 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 bindi...

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Bibliographic Details
Published inEnzyme (Basel) Vol. 24; no. 2; pp. 132 - 136
Main Authors Arneson, R.M, Geller, A.M, Byrne, W.L
Format Journal Article
LanguageEnglish
Published Switzerland 01.01.1979
Subjects
Adenosine Monophosphate
animal science
Animals
Cattle
Fructose-Bisphosphatase - metabolism
Kinetics
Liver - enzymology
livestock
Protein Binding
zoology
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Summary:Bovine liver fructose 1,6-bisphosphatase bound 4 mol of its allosteric inhibitor AMP per mole of enzyme with half-saturation at 17 mumol/l 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: K1' less than K2' greater than K3' less than K4', indicating mixed cooperativity.
ISSN:0013-9432
DOI:10.1159/000458641