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Human liver N-acetyltransferase was purified by means of column chromatography on Sephadex G-100 (18 fold; yield: 60-70%) and preparative disc electrophoresis (40 fold; yield: 95 - 100%). A separation of the hypothetical “serotonin-N-acetyltransferase” and “INH-N-acetyltransferase” on the basis of a possible difference of the charge of the proteins could not be achieved (disc electrophoresis). Thus the assumption is confirmed that INH and Serotonin are substrates of one enzyme.

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Anreicherung der Leber-N-Acetyltransferase durch präparative Polyacrylamidgel-Elektrophorese und Bestimmung des Molekulargewichts /Purification of Human Liver Serotonin-/Isoniazid-N-Acetyltransferase by Preparative Polyacrylamidgel-Electrophoresis and Determination of Molecular Weight