Succinic semialdehyde dehydrogenase: Purification and properties of the enzyme from monkey brain

DPN-dependent succinic semialdehyde dehydrogenase from rhesus monkey brain retains full activity when purified by fractionation in the absence of reducing agents. In this state, the enzyme is relatively insensitive to arsenite. Addition of mercaptoethanol markedly increases the arsenite sensitivity. Both DPN and mercaptoethanol are effective in protecting the enzyme from auto-oxidation. Additional experiments are presented in support of a role of DPN in stabilizing the tertiary structure of the enzyme in the vicinity of the aldehyde binding site.