Abstract
The aminopeptidase activity in the brain which converts vasopressin into centrally active metabolites, was quantitated on basis of the release of 3H-Phe from the substate [3H-Phe3]vasopressin and separation by hydrophobic interaction chromatography on mini-columns. After subcellular fractionation of whole rat brain homogenates the highest specific activity of the peptidase was recovered in membrane fractions, in particular microsomes and the P3 fraction, and the cytosol. The peptidase activity was present in all brain areas. Highest activity was measured in membranes of the bulbus olfactorius, preoptical area and cerebellum. Lowest activity was found in the medulla oblongata and striatum. The peptidase activity is not restricted to the vasopressin system per se, but may have a more general role in neuropeptide metabolism.
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