Abstract
The glutathione S-transferase present in the adult worker bee Apis mellifera macedonica was purified and analyzed for its physicochemical and kinetic properties. The enzyme is heterodimeric with subunit molecular masses of 29 and 25 kDa, respectively. Two main isoenzymes with distinct kinetic properties are present, with isoelectric points of 7.40 for the alkaline and 4.58 for the acidic forms, respectively. The two enzymes are induced independently by factors such as insecticide treatments and environmental conditions, including low temperatures or starvation.
MeSH terms
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Animals
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Bees / enzymology*
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Cold Temperature*
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Dimerization
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Electrophoresis, Polyacrylamide Gel
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Enzyme Induction
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Enzyme Inhibitors / pharmacology
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Glutathione Transferase / biosynthesis
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Glutathione Transferase / chemistry
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Glutathione Transferase / drug effects
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Glutathione Transferase / isolation & purification
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Glutathione Transferase / metabolism*
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Hydrogen-Ion Concentration
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Insecticides / pharmacology
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Isoelectric Point
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Isoenzymes / biosynthesis
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Isoenzymes / chemistry
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Isoenzymes / drug effects
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Isoenzymes / isolation & purification
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Isoenzymes / metabolism
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Kinetics
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Molecular Weight
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Nitriles
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Paraoxon / analogs & derivatives*
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Paraoxon / pharmacology
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Pyrethrins / pharmacology
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Sensitivity and Specificity
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Substrate Specificity
Substances
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Enzyme Inhibitors
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Insecticides
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Isoenzymes
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Nitriles
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Pyrethrins
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decamethrin
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Glutathione Transferase
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Paraoxon
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methylparaoxon