Department of Agricultural Chemistry, National Taiwan University, and Institute of Biological Chemistry, Academia Sinica.
Plant Physiol. 1977 Jul;60(1):17-21. doi: 10.1104/pp.60.1.17.
A 108-fold purification of the sucrose synthetase from the extract of the shoot of bamboo Lelaba oldhami was achieved by ammonium sulfate fractionation, calcium phosphate gel adsorption, and chromatographic separations on Sephadex G-100 and diethylaminoethyl-cellulose columns. Some properties of this enzyme, namely thermal and pH stabilities, stabilization by aqueous glycerol, pH optimum, substrate specificities, effects of metallic ions, effects of sulfhydryl reagents, molecular weight, sedimentation constants, isoelectric point, and substrate saturation kinetics had been investigated.The substrate saturation kinetics indicated that the enzyme could be an allosteric enzyme with the saccharide substrates (sucrose and fructose) serving as the homotropic allosteric effectors in regulating the biosynthesis and degradation of sucrose.
从龙竹 shoot 提取物中,通过硫酸铵分级沉淀、磷酸钙凝胶吸附以及葡聚糖凝胶 G-100 和 DEAE-纤维素柱层析等方法,实现了蔗糖合酶的 108 倍纯化。该酶的一些性质,如热稳定性和 pH 稳定性、水甘油稳定、最适 pH 值、底物特异性、金属离子效应、巯基试剂效应、分子量、沉降常数、等电点以及底物饱和动力学等已被研究。底物饱和动力学表明,该酶可能是一种变构酶,糖底物(蔗糖和果糖)作为同型变构效应物,调节蔗糖的生物合成和降解。