Department of Agronomy, University of Missouri, Columbia.
Planta. 1972 Dec;103(4):361-4. doi: 10.1007/BF00386709.
Glucosyltransferase activity was extracted from maize pollen in distilled water. The enzymatic reaction required UDP-glucose, mercaptoethanol and Ca(++), and had a pH optimum at 8.2. Either kampferol or quercetin served as a substrate. Michaelis-Menten constants obtained were 0.6×10(-4) M for quercetin and 0.74×10(-3)M for UDP-glucose. Ammonium-sulfate precipitation of the enzyme gave a 4fold purification.
葡糖基转移酶活性从蒸馏水中的玉米花粉中提取。该酶促反应需要 UDP-葡萄糖、巯基乙醇和 Ca(++),最适 pH 值为 8.2。山奈酚或槲皮素均可作为底物。得到的米氏常数分别为 0.6×10(-4) M 对槲皮素和 0.74×10(-3) M 对 UDP-葡萄糖。酶的硫酸铵沉淀可使酶纯化 4 倍。