반하(Pinellia ternata) 뿌리를 $4^{circ}C$에서 생리식염수로 추출한 후 hydroxyapatite 및 CM-cellulose column chromatography에 의하여 순수한 단백질의 lectin을 분리 정제하였다. Sephadex G-100 gel 여과법을 통하여 측정한 바 lectin의 분자량은 약 160,000이었으며 glycoprotein이 아니며 subunit도 없는 monomer로 존재하고 있는 순수한 단백질이었다. 본 lectin은 사람의 적혈구(A,B,O형)와는 아무런 응집반응도 일으키지 않으나 토끼나 생쥐 또는 흰쥐와 같은 동물들의 적혈구와는 응집반응을 일으키는 특성을 가지고 있었다. 응집반응이 일어나는 pH의 범위는 4.5~9.0이며 흰쥐에 있어서 최적pH 는 7.0~7.2였다. 응집반응에는 2가 양이온이 관여하지 않았으며 반응을 저해하는 "당"도 발견되지 않았다. 본 lectin은 열에 대한 안정도가 높아서 $100^{circ}C$에서 25분 정도 처리하여야 응집성이 소실되었다.
In order to study the chemical characteristics of Banha (Pinellia ternata) lectin, the lectin was extracted from Banha roots using saline method at $4^{circ}C$ and purified by hydroxyapatite and CM-cellulose column chromatography. The purity of Banha lectin was ascertained by Davis and SDS-polyacrylamide gel electrophoresis and double gel diffusion method. The molecular weight of purified lectin was estimated as 160,000 by the method of Sephadex G-100 gel filtration. The lectin was certainly a pure monomeric nonglycoprotein having no subunit. In the hemagglutination test for the lectin, hemagglutination was not observed in the human erythrocytes (A,B,O) even by treatment with trypsin. The lectin, however, reacted with erythrocytes of animals such as rabbit, mouse and rat, and showed a hemagglutination phenomena. Hemagglutination occured at pH range from 4.5 to 9.0 and the optimal range was from 7.0 to 7.2. For the agglutination, divalent cations were not required and no monosaccahride was found to be a inhibitor. The lectin had a strong thermal stability and thus its agglutinating ability was eventually lost after being treated at $100^{circ}C$ for 25 minutes.
