효소 단백질에 대한 탄닌의 특이적 흡착성질과 흡착 크로마토그래피의 응용성에 대하여 검토하였다. 고정화 탄닌 1 g당 nuclease $P_1$의 흡착량은 40 mg 이었으며, 흡착된 nuclease $P_1$을 90%의 높은 수율로 회수할수 있었다. 황산 암모니움 염석과 단백질 정제의 새로운 시도방법으로서 탄닌 흡착 크로마토그래피에 의하여 nuclease $P_1$의 부분정제를 시도한 결과 nuclease $P_1$의 비활성은 15.6 배 향상되었으며, 이때 수율은 55.3% 였다.
As a new approach for protein purification, affinity characteristics of tannin for enzyme protein and its applicability to adsorption chromatography were investigated. Crude nuclease $P_1$ was first purified by fractionation of ammonium sulfate followed by tannin adsorption chromatography. Result showed that adsorption capacity of nuclease $P_1$ onto one gram of immobilized tannin was 40 mg and recovery yield of the enzyme was 90%. Specific activity of the purified nuclease $P_1$ increased to 15.6 fold higher than that of crude extract, recovering 55.3% of enzyme yield.
