Some characteristics of a purified heat-stable aldolase.
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.
D000446:Aldehyde-Lyases; D001407:Bacillus; D001419:Bacteria; D005634:Fructose-Bisphosphate Aldolase; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006435:Renal Dialysis
D000446:Aldehyde-Lyases; D005634:Fructose-Bisphosphate Aldolase
ALDEHYDE-LYASES; BACILLUS