Abstract
THE naturally-occurring pentapeptides leucine- and methi-onine-enkephalin which exhibit agonist activity at the opiate receptor1 are subject to rapid deactivation by tissue homogenates2,3. The primary mode of degradation has been demonstrated to be cleavage of the Tyr–Gly amide bond4,5. It is not surprising, therefore, that the opiate actions of the exogenously administered peptides are transient6–9 and the biological half life of the peptides is very short. We have previously studied degradation of the enkephalins in relatively crude preparations and we present here a study of the subcellular localisation of enkephalin-hydrolysing activity (EHA) in rat brain. We found a heterogenous distribution of EHA in rat brain subfractions and evidence for enzyme heterogeneity. Opiate receptors are apparently functionally unrelated to the site of EHA in synaptic membranes.
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LANE, A., RANCE, M. & WALTER, D. Subcellular localisation of leucine-enkephalin-hydrolysing activity in rat brain. Nature 269, 75–76 (1977). https://doi.org/10.1038/269075a0
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DOI: https://doi.org/10.1038/269075a0
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