CYTOCHROME OXIDASE IN CELLS OF THE GENUS BRUCELLA

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Abstract
Conditions were selected to permit the quantitative determination of cytochrome oxidase activity of brucellae. Oxygen uptake of a given number of cells at pH 6.2 and in the presence of 0.07 [image]p-phenylenediamine is approximately 4 times greater than that obtained at pH 7.3 in 0.02 [image] reductant, the conditions generally used for measuring cytochrome oxidase activity. Activity was expressed as microliters of oxygen taken up by 109 viable cells per hour. The cytochrome oxidase activity of 24 thionin-sensitive strains of Brucella abortus was 22.5 to 33.0; the activity of 4 thionin-resistant strains of B. abortus was 9 to 12; the activity of 15 strains of B. melitensis was 7.5 to 24.5; the activity of 22 strains of Brucella suis was 5.0 to 14.5. Although the degree of cytochrome oxidase activity differentiated recently isolated, typical B. abortus from B. suis, it did not permit their differentiation from B. melitensis.