Involvement of endo-oligopeptidases A and B in the degradation of neurotensin by rabbit brain.
Incubation of neurotensin with rabbit brain cytosol fractions resulted in a rapid loss of carboxy-terminal neurotensin immunoreactivity, whereas the amino-terminal portion of neurotensin was relatively stable to degradation. Neurotensin degradation by rabbit brain cystosol fractions was activated by dithiothreitol and inhibited by thiol blocking reagents, Zn2+, and by monospecific antibodies against endo- oligopeptidases A and B, thus suggesting the possible involvement of these enzymes in neurotensin degradation by rabbit brain. An association of a proportion of endo- oligopeptidase B activity (proline endo-peptidase) with the membrane fraction of nervous tissue was suggested by the presence of proline endopeptidase activity on the membranes and by immunoprecipitation of the solubilized activity using anti-endo- oligopeptidase B antiserum.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D003546:Cysteine Endopeptidases; D003600:Cytosol / Q000201:enzymology; D010450:Endopeptidases / Q000378:metabolism*; D007700:Kinetics; D009496:Neurotensin / Q000378:metabolism*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D011817:Rabbits; D012995:Solubility
D009496:Neurotensin; D010450:Endopeptidases; D007703:Peptidyl-Dipeptidase A; D003546:Cysteine Endopeptidases; C028307:endopeptidase B