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

Peptides, Vol. 15, No. 5, p. 933, 1994 Copyright © 1994 Elsevier Science Ltd Printed in the USA. All fights reserved 0196-9781/94 $6.00 + .00

Pergamon

Erratum BURBACH, J. P. H., F. M. DE BREE, D. TERWEL, A. TAN, H.-P. MASKOVA AND A. A. M. VAN DER KLEIJ. Properties ofaminopeptidase

activity involved in the conversion of vasopressin by rat brain membranes. PEPTIDES 14(4) 807-813, 1993.--

Table 1 contained four relative activity errors. We are reprinting the corrected table here and regret any inconvenience caused by this error. TABLE

1

EFFECT OF PEPTIDASE INHIBITORS ON VP-AP ACTIVITY IN RAT BRAIN MEMBRANES Compound

Concentration

None PMSF Aprotinin Iodoacetamide N-Ethylmaleimide PCMB PCMBS EDTA 1,10-phenanthroline

-1 mM 100 #g/ml 1 mM 0.1 m M 0.1 m M 0.1 m M 0.1 m M 0.1 m M 1 mM 0.1 m M 1 mM 1 mM 10 m M 20 #g/ml 100 #g/ml 100 #g/ml 20 #g/ml 100 #g/ml 0.1 m M 1 mM 0.0! m M 0.1 m M 1 mM 0.01 m M 0.1 m M 1 mM

Dithiothreitol /5-Mercapthoethanol Antipain Leupeptin Bacitracin Puromycin Bestatin

Amastatin

Relative Activity* (%) 100 85 95 53 50 22 23 19 73 8 260 400 190 340 79 52 84 66 40 73 20 66 29 14 55 13 2

* VP-AP activity was determined in 62 m M NaCI, 40 m M Tris-HC1, pH 7.0, at a membrane protein concentration of 1.3 mg/ml by incubation for 20 min, 37°C. Compounds were preincubated for 10 min. The enzyme activity measured in the absence of inhibitor is taken as 100%.

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