Carboxypeptidase activity in synaptic vesicles isolated from striatum and cortex of calf brain.
A carboxypeptidase activity has been found in synaptic vesicles (secretory granules) isolated from the cortex and striatum of calf brain which removes amino acids from the carboxy terminus of enkephalin-containing (EC) peptides. The formed enkephalin molecules are not further degraded by this enzyme activity. The preparations were found to be free of cytoplasmic and lysosomal constituents as determined by marker enzyme activities. The vesicle preparations of both cortex and striatum showed differences in the degradation velocities of the various EC peptides depending on size and charge of the amino acid present at the carboxy terminus. The pH optimum of the release of Met-enkephalin from Met-enkephalin-Arg6 has been shown to be between pH 5 and 6. The enzyme activity is inhibited by thiol-blocking agents such as p-hydroxymercuribenzoate and copper ions, but only slightly by metal-chelating agents.
D000818:Animals; D002268:Carboxypeptidases / Q000032:analysis*; D002417:Cattle; D002540:Cerebral Cortex / Q000201:enzymology*; D002729:Chloromercuribenzoates / Q000494:pharmacology; D003300:Copper / Q000494:pharmacology; D003342:Corpus Striatum / Q000201:enzymology*; D004744:Enkephalin, Methionine / Q000031:analogs & derivatives / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011480:Protease Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity; D013572:Synaptic Vesicles / Q000201:enzymology*; D020245:p-Chloromercuribenzoic Acid
D002729:Chloromercuribenzoates; D011480:Protease Inhibitors; D004744:Enkephalin, Methionine; D020245:p-Chloromercuribenzoic Acid; C028719:enkephalin-Met, Arg(6)-; D003300:Copper; D002268:Carboxypeptidases