Enzymic hydrolysis of phosphonate esters.
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Acid Phosphatase↗
Biomedical subjects
L G Butler
Publications and source records attributed to L G Butler.
Enzyme immobilization by adsorption on hydrophobic derivatives of cellulose and other hydrophilic materials.
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Alkaline Phosphatase↗
Evidence for a convalent intermediate between alpha-glucosidase and glucose.
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Animals↗
Stimulation of alkaline phosphatase by analogs of inorganic pyrophosphate.
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Alkaline Phosphatase↗
Kinetic effects of inorganic pyrophosphate analogs on several inorganic pyrophosphate hydrolyzing enzymes.
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Alkaline Phosphatase↗
Yeast inorganic pyrophosphatase. VI. Studies on specificity and mechanism.
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Binding Sites↗
Maize leaf inorganic pyrophosphatase: isozymes, specificity for substrates, inhibitors, and divalent metal ions, and pH optima.
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Cations, Divalent↗
Yeast inorganic pyrophosphatase. I. Binding of pyrophosphate, metal ion, and metal ion-pyrophosphate complexes.
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Binding Sites↗
Yeast inorganic pyrophosphatase. 3. Kinetics of Ca 2+ inhibition.
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Binding Sites↗
Yeast inorganic pyrophosphatase. II. Kinetics of Mg 2+ activation.
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Binding Sites↗
Photoinactivation of microsomal glucose-6-phosphatase.
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Animals↗
Protein-bound phosphoryl histidine: a probable intermediate in the microsomal glucose-6-phosphatase-inorganic pyrophosphatase reaction.
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Animals↗
Yeast inorganic pyrophosphatase. IV. Purification, quaternary structure, and evidence for strongly bound Mg 2+1 .
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Binding Sites↗
Hydrolysis of acyl phosphates by alkaline phosphatases.
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Acetates↗
Detection and characterization of the phosphorylated form of microsomal glucose-6-phosphatase.
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Animals↗
Measurement of binding of phosphate ligands to ribonuclease A by direct and competive dialysis rate techniques.
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Binding Sites↗
Alkaline inorganic pyrophosphatase of maize leaves.
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Albinism↗
Inorganic pyrophosphatase of rat liver mitochondria. Correlation of latency with catalytic properties and intramitochondrial location.
Stimulation of Mg(2+)-dependent inorganic pyrophosphatase activity several fold by disruption of mitochondrial membranes does not appreciably alter the catalytic properties of the enzyme. Stimulation is due to increased accessibility of substrate to the enzyme, which is not solublized on activation. The enzyme is attached to the inside of the inner membrane, and under physiological conditions probably hydrolyzes only intramitochondrially-produced PP(i).
Adenosine Triphosphatases↗