Aldolase activity in the cell-free extract of the protozoan Leishmania donovani

Abstract

Aldolase has been shown to be present in the cell-free extract of Leishmania donovani. In view of its metal requirement and other properties it resembles the class I type of aldolases. Unlike bacterial aldolase, however, it is not inhibited by α,α'-dipyridyl and EDTA. It is insensitive to the well-known -SH reagents. It is strongly inhibited by Cu²⁺ ions and to a lesser degree by Zn²⁺ and Mn²⁺ ions. The optimum pH of the enzyme is 7.2.