Journal of Bacteriology · 1962 · 19 citations · 10 references
Life SciencesBiochemistryMicrobiologyEnzyme MechanismEnzymologyMicrobial MetabolismEnzyme AssaysEnzyme CharacterizationEnzyme InhibitionEnzyme KineticsEnzyme StabilityThermostable EnzymesAssayAssay SpecificityChelate EffectEnzyme Thermal StabilityTemperature Dependence Of Enzyme ActivityTemperature Effects On Enzyme ActivityThermophilic CulturesThermophilic Microorganisms
Thompson, P. J. (University of Nebraska, Lincoln) and T. L. Thompson. Some characteristics of a purified heat-stable aldolase. J. Bacteriol. 84:694-700. 1962-Aldolase from a thermophilic strain of bacteria was obtained in a state of high purity. Heat studies of purified aldolases from cells cultivated at 45 and 65 C showed them equally stable at 70 C for 1 hr. Metal-ion and chelate studies indicated that thermal aldolase is metal ion-independent. Carboxypeptidase did not alter activity or specificity. The enzyme was specific for fructose-1,6-diphosphate. Hydrazine was found inhibitory in the assay procedure. The inhibition was independent of pH over the range of H(+) concentrations tested and was reversed by dialysis against water.
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