PMID: 7993391Jul 1, 1993Paper

Properties of aminopeptidase activity involved in the conversion of vasopressin by rat brain membranes

J P BurbachA A Van der Kleij


Previously it has been shown that vasopressin (VP) and oxytocin are converted by aminopeptidase activity in brain membranes into fragments with potent CNS activities. This report concerns the properties of this enzyme activity, addressed as VP-converting aminopeptidase (VP-AP) activity, in membranes of the rat brain. The VP-AP activity had a pH optimum at pH 7.0 and had a Km of 17 microM for its action on VP. Amastatin was the most potent aminopeptidase inhibitor. Enzyme activity was inhibited by relatively low concentrations of metal chelators. Treatment of brain membranes by EDTA resulted in loss of enzyme activity that was completely reversed by 10 microM Zn2+, indicating that VP-AP activity is a metallopeptidase. Several VP analogues and fragments, in particular VP(1-8), inhibited the action of enzyme activity on VP. Among peptides unrelated to VP, angiotension I, somatostatin, and porcine ACTH(1-39) markedly inhibited enzyme activity. Solubilization of VP-AP activity from brain membranes and gel filtration on Sephadex G200 showed two peaks of activity, one eluting with an apparent mass of about 140 kDa, the other in the void volume. Gel filtration fractions were able to convert [3H][Phe3]VP in a step-wise fashion. The VP-A...Continue Reading


Mar 1, 1977·Journal of Biochemistry·M Hayashi, K Oshima
Feb 28, 1979·Biochemical and Biophysical Research Communications·J P BurbachD de Wied
Feb 1, 1976·Pharmacological Research Communications·W B WatkinsR Walter
Jan 1, 1991·Neuroscience and Biobehavioral Reviews·A Argiolas, G L Gessa
Apr 29, 1987·Biochemical and Biophysical Research Communications·J P BurbachJ L Lebouille
Oct 14, 1983·European Journal of Pharmacology·J P BurbachD De Wied

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