Univalent cation activation of fructose 1,6-diphosphatase
| Autor: | Ana Maria Gonzalez, Julieta Villanueva, Elizabeth Hubert, Frank Marcus |
|---|---|
| Rok vydání: | 1970 |
| Předmět: |
Bromides
Chemical Phenomena Swine Biophysics Acetates Kidney Biochemistry Phosphates chemistry.chemical_compound Chlorides Fructose 1 6 diphosphatase Animals Raja chilensis Magnesium Tromethamine Molecular Biology chemistry.chemical_classification Nitrates Adenine Nucleotides Sulfates Chemistry Muscles Pig kidney Sodium Fishes Fructose Hydrogen-Ion Concentration Fructose-Bisphosphatase Enzyme Activation Quaternary Ammonium Compounds Enzyme Liver Metals Potassium Fish Rabbits |
| Zdroj: | Archives of Biochemistry and Biophysics. 138:590-597 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(70)90385-1 |
| Popis: | Fructose 1,6-diphosphatase from several vertebrate sources has been studied with respect to univalent cation activation. All the enzymes tested showed activation by certain univalent cations, K + or NH 4 + being the best activators. A re-evaluation of some properties of fructose 1,6-diphosphatases in the presence of univalent cation activators showed, as studied with pig kidney, rabbit liver, and rabbit muscle fructose 1,6-diphosphatase, that the Mg 2+ -saturation curves were markedly altered by the presence of 150 m m K + . Not only an increase in K a and V max was observed, but also the sigmoidal nature of the Mg 2+ -saturation curves became evident. AMP inhibition, characteristic of most fructose 1,6-diphosphatases, was not significantly altered by the presence of K + in the case of pig kidney, rabbit liver, and fish ( Raja chilensis ) liver fructose 1,6-diphosphatase. Rabbit muscle fructose 1,6-diphosphatase became more sensitive to AMP inhibition, while in the case of fish ( Genipterus chilensis ) liver fructose 1,6-diphosphatase, inhibition by AMP could only be demonstrated in the presence of the univalent cation activators. |
| Databáze: | OpenAIRE |
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