아세톤으로 탈지한 대두분으로부터 gel여과법과 이온 교환 크로마토그래피등의 전통적인 단백질 추출 방법을 이용하여 Lipoxygenase 이성효소를 분리하였다. 이온 교환 후의 lipoxygenase-1과 -2는 Crude extract에 비해 각각 19배와 32배 정제 되어졌으나, 상당한 효소활성의 손실을 초래하였으며, lipoxygenase 에 특이적인 염색기술을 이용하여 행한 7% PAGE에서 lipoxygenase-1, -2, 그리고 -3은 각각 0.38, 0.29그리고 0.33의 Rf치를 나타내었다.
Soybean lipoxyeenase isozymes were isolated from acetone-defatted soybean seeds(Glycine max [L.] Merr. variety AmSoy) by ammonium sulfate fractionation, eel filtration, and ion exchange chromatoeraphy. The final preparation of lipoxygenase-1 and -2 obtained was 19- and 32-fold purified, respectively, to the crude extract. But a considerable loss of total enzyme activity occurred during purification. On 7% polyacrylamide gel electrophosis at pH 9.0, employing lipoxigenase specific staining technique, lipoxyeenase-1, -2, and -3 showed distinctive Rf values of 0.38, 0.29, and 0.33, respectively.
