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朝鲜花冠小月螺的内脏提取液,经盐析透析、DEAE纤维素柱层析,分离得三个酶峰,分别称之酶Ⅰ、酶Ⅱ和酶Ⅲ.再经Sephadex G-25凝胶过滤,得三种较纯的酶,最大提纯了73倍. 对三种酶的动力学性质分别进行试验,最适pH:酶Ⅰ为7.6±0.02 Tris-HCl缓冲液,酶Ⅱ为6.6±0.02 Na2HPO4-NaH2PO4缓冲液,酶Ⅲ为5.6±0.02HAc-NaAc缓冲液.在试验浓度范围内,KCl和NaCl对三种酶都是激活剂;MnCl2对三种酶都是抑制剂;MgCl2对酶Ⅰ和酶Ⅱ为激活剂,高浓MgCl2对酶Ⅲ为抑制剂;Pb(OAc)2对三种酶的作用不同.三种酶的Km值依次为0.2、0.6和0.04mg/ml. 相似文献
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The crude enzyme, which was extracted from viscera of Lunella coronata coreensis (Recluz), was salted out and dialysed. Three enzymatic peaks isolated from DEAE-cellulose column chromatography were refered to as lyase Ⅰ, Ⅱ and Ⅲ, respectively. Then these lyases underwent gel-filtration on Sephadex G-25 respectively, and three purer lyases were derived therefrom, the highest purification being 73 fold.The kinetics of the three lyases was tested respectively. The optimum pH was as follows: lyase Ⅰ was 7.6±0.02 Tris-HCl buffer; lyase Ⅱ was 6.6±0.02 Na2HPO4-NaH2PO4 buffer; and lyase Ⅲ was 5.6±0.02 HAc-NaAc buffer. In the rang of tested concentration, KC1 and Nad were the activator and MnCl2 was the inhibitor, all for the three lyases; MgCl2 was the activator for lyases Ⅰ and Ⅱ, but the MgCl2 of high concentration was the inhibitor for lyase Ⅲ; Pb (OAc)2 acted differently for three lyases. The Km values of these lyases were 0.2, 0.6 and 0.04 mg/ml in order of precedence. 相似文献
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