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. 1962 Oct;84(4):694-700.
doi: 10.1128/jb.84.4.694-700.1962.

Some characteristics of a purified heat-stable aldolase

P J THOMPSON, T L THOMPSON

Some characteristics of a purified heat-stable aldolase

P J THOMPSON et al. J Bacteriol. 1962 Oct.

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.

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