The purification and properties of placental histaminase

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Abstract
Histaminase was extracted from desanguinated human placentae and purified by salt fractionation, ion-exchange chromatography and gel filtration. The purest preparation was still contaminated with haptoglobin-methaemoglobin. Histaminase activity was measured by the o-aminobenzaldehyde method of Holmstedt & Tham (1959), Kapeller-Adler''s (1951) test and a modified spectrophotometric indi-godisulphonate test of greater sensitivity. Unless contaminant metal ions were removed, enzymic activity on cadaverine, but not on hist-amine, fell during purification. When EDTA was added to the working buffers, a constant ratio between activities towards cadaverine and histamine was maintained throughout the later stages of purification, and activities towards the two substrates could not be separated by any of the highly resolving chromatographic analyses employed. The purest preparation oxidized histamine, agmatine and benzylamine more slowly than the C4-C6 aliphatic diamines, but mixed-substrate experiments suggested that all these amines were substrates of histaminase. The substrate and inhibitor specificities of placental histaminase were compared with those of related enzymes from other sources.