[HTML][HTML] Autocatalytic processing of recombinant human procathepsin L: Contribution of both intermolecular and unimolecular events in the processing of procathepsin …
R Ménard, E Carmona, S Takebe, E Dufour… - Journal of Biological …, 1998 - ASBMB
The autocatalytic processing of procathepsin L was investigated in vitro using purified
recombinant proenzyme expressed in Pichia pastoris. Pure intermolecular processing was
studied by incubating the mutant procathepsin L (C25S), which cannot autoactivate with a
small amount of mature active cathepsin L. The results clearly establish that, contrary to
recent reports, intermolecular processing of procathepsin L is possible. The main cleavage
sites are located at or near the N terminus of the mature enzyme, in an accessible portion of …
recombinant proenzyme expressed in Pichia pastoris. Pure intermolecular processing was
studied by incubating the mutant procathepsin L (C25S), which cannot autoactivate with a
small amount of mature active cathepsin L. The results clearly establish that, contrary to
recent reports, intermolecular processing of procathepsin L is possible. The main cleavage
sites are located at or near the N terminus of the mature enzyme, in an accessible portion of …