Abstract
Inactivation of rabbit liver fructose 1,6-bisphosphatase (Fru-P 2ase, EC 3.1.3.11) by a membrane-bound lysosomal proteinase, designated as cathepsin M, is reversed by incubation with cystamine, which has been shown to form a mixed disulfide derivative with protein SH groups. The native form of Fru-P 2ase is also activated by cystamine; this activated form is resistant to the action of membrane-bound cathepsin M.
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