Article
The use of triphenyltetrazolium chloride in the study of dehydrogenase activity of Brucellae
O emprêgo do cloreto de trifeniltetrazólio no estudo da atividade dehidrogenásica de brucelas
Registro en:
MELLO, Milton Thiago de; SILVA, Niber Paz M. The use of triphenyltetrazolium chloride in the study of dehydrogenase activity of Brucellae. Memórias do Instituto Oswaldo Cruz, Rio de Janeiro, v. 53, n. 1, p. 1 - 14, 1955.
0074-0206
10.1590/S0074-02761955000100006
1678-8060
Autor
Mello, Milton Thiago de
Silva, Niber Paz M.
Resumen
Experiments for the investigation of dehydrogenase activity of washed cells of a strains of Br. abortus and another of Br. suis in presence of different single added substrates are reported. The activity was measured as the amount of formazan produced by the reduction of 2, 3, 5-triphenyltetrazolum chloride acting as a hydrogen ions acceptor, at pH 7.0. In a general manner the dehydrogenase activity of Br. suis was much more intense than that of Br. abortus (fig. 5). In the conditions of the experiments Br. abortus oxidized L-arabinose, D-galactose, D-glucose, glycerol, D-xylose, DL-alanine, D-fructose, and D-sorbitol. Brucella suis oxidized D-xylose, L-arabinose, D-glucose, D-galactose, DL-alanine, sodium acetate, maltose, glycine, D-fructose, and D-sorbitol. Glycerol was oxidized by Br. abortus but its oxidation by Br. suir was very slight. Sodium acetate and maltose were intensely oxidized by Br. suir but not by Br. abortus. The sites of more intense enzymatic acitivity were seen as small red colored round granules located in one pole of the cells.