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J Bacteriol. 1962 October; 84(4): 694-700
Copyright © 1962, The Williams & Wilkins Company. All Rights Reserved.

SOME CHARACTERISTICS OF A PURIFIED HEAT-STABLE ALDOLASE

^a Department of Microbiology, University of Nebraska, Lincoln, Nebraska

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.

¹ Present address: Department of Bacteriology, Northwestern State College of Louisiana, Natchitoches.

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