Papers in the Biological Sciences
Date of this Version
May 1962
Abstract
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.
Comments
Published in Journal of Bacteriology, volume 84, 1962. Copyright © 1962 by the American Society for Microbiology. Used by permission.