SOME CHARACTERISTICS OF A PURIFIED HEAT-STABLE ALDOLASE
AUTOR(ES)
Thompson, P. J.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=277945Documentos Relacionados
- Some properties of purified Escherichia coli heat-stable enterotoxin II.
- Immunological properties of purified Klebsiella pneumoniae heat-stable enterotoxin.
- Characteristics of heat-stable extracellular hemolysin from Pseudomonas aeruginosa.
- Escherichia coli heat-stable enterotoxin: rapid method of purification and some characteristics of the toxin.
- Enteroaggregative Escherichia coli heat-stable enterotoxin 1 represents another subfamily of E. coli heat-stable toxin.
