Activation and stabilization of asparaginase by anti-asparaginase IgG and its Fab.
Modified asparaginase, in which 4 tryptophan residues were modified with 2-hydroxy-5-nitrobenzyl bromide, had little enzymic activity and retained immunoreactivity [(1976) FEBS Lett. 65, 11-15]. Addition of IgG or its Fab towards asparaginase to the modified asparaginase gave rise to marked enhancement of the enzymic activity. Native asparaginase (4 subunits) lost the enzymic activity due to dissociation into subunits by dilution of the enzyme solution. However, in the presence of Fab, asparaginase did not lose enzymic activity on dilution, probably due to no dissociation into subunits occurring.
D000936:Antigen-Antibody Complex; D001215:Asparaginase / Q000276:immunology* / Q000378:metabolism; D001665:Binding Sites; D004789:Enzyme Activation; D007140:Immunoglobulin Fab Fragments / Q000276:immunology*; D007074:Immunoglobulin G / Q000276:immunology*; D046911:Macromolecular Substances; D011487:Protein Conformation
D000936:Antigen-Antibody Complex; D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G; D046911:Macromolecular Substances; D001215:Asparaginase