Histaminase was partially purified by Sephadex G-200 gel filtration at high temperature. Guinea pig liver histaminase was extracted with heparin. The extract was fractionated by Sephadex G-200 gel filtration at 4°C. In the fractions containing histaminase, 7 dense and 2 faint protein bands were detected on SDS-gel electrophoresis. Further, fractionation of this sample by Sephadex G-200 gel filtration at 55°C markedly decreased the number of bands, i.e. only 1 dense and 2 faint bands were observed in the fractions in which histaminase activity was detected, and the enzyme activity was increased by approximately ten times. The results suggest that gel filtration at high temperature may be useful for partial purification of histaminase.