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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Velasco P, Barcia R, Ibarguren I, Sieiro A M, Ramos-Martinez J I

Departmento de Bioquimica y Biología Molecular, Universidad de Santiago de Compostela, Facultad de Veterinaria, Lugo, Spain.

Int J Biochem. 1994 Feb;26(2):195-200. doi: 10.1016/0020-711x(94)90145-7.

Glucose-6-phosphate dehydrogenase (G6PDH EC 1.1.1.49) from mouse liver has been purified 1100-fold by extraction, ion-exchange chromatography on DE-52, absorption chromatography on Bio-Gel HTP and gel filtration through sepharose 6 HR 10/30. The purified enzyme showed a single band in silver stained SDS-PAGE. 2. The native and subunit molecular weight were 117 and 31 kDa respectively. 3. The kinetic studies and the patterns obtained from the inhibition by-products suggest that the enzyme follows an ordered sequential kinetic mechanism. 4. The reduced Km values for the substrates favour the operativity of the enzyme. The "fine control" of the enzymatic activity was exerted by the NADPH, whose Ki is several fold lower than the in vivo concentration.

从小鼠肝脏中提取的葡萄糖-6-磷酸脱氢酶（G6PDH，EC 1.1.1.49），通过在DE-52上进行离子交换色谱、在Bio-Gel HTP上进行吸附色谱以及通过琼脂糖6 HR 10/30进行凝胶过滤，已被纯化了1100倍。纯化后的酶在银染SDS-PAGE中显示为单一条带。2. 天然分子量和亚基分子量分别为117 kDa和31 kDa。3. 动力学研究以及从抑制副产物获得的模式表明，该酶遵循有序的顺序动力学机制。4. 底物的降低的Km值有利于酶的活性。酶活性的“精细控制”由NADPH施加，其Ki比体内浓度低几倍。

Velasco P, Barcia R, Ibarguren I, Sieiro A M, Ramos-Martinez J I

Departmento de Bioquimica y Biología Molecular, Universidad de Santiago de Compostela, Facultad de Veterinaria, Lugo, Spain.

Int J Biochem. 1994 Feb;26(2):195-200. doi: 10.1016/0020-711x(94)90145-7.

Glucose-6-phosphate dehydrogenase (G6PDH EC 1.1.1.49) from mouse liver has been purified 1100-fold by extraction, ion-exchange chromatography on DE-52, absorption chromatography on Bio-Gel HTP and gel filtration through sepharose 6 HR 10/30. The purified enzyme showed a single band in silver stained SDS-PAGE. 2. The native and subunit molecular weight were 117 and 31 kDa respectively. 3. The kinetic studies and the patterns obtained from the inhibition by-products suggest that the enzyme follows an ordered sequential kinetic mechanism. 4. The reduced Km values for the substrates favour the operativity of the enzyme. The "fine control" of the enzymatic activity was exerted by the NADPH, whose Ki is several fold lower than the in vivo concentration.

从小鼠肝脏中提取的葡萄糖-6-磷酸脱氢酶（G6PDH，EC 1.1.1.49），通过在DE-52上进行离子交换色谱、在Bio-Gel HTP上进行吸附色谱以及通过琼脂糖6 HR 10/30进行凝胶过滤，已被纯化了1100倍。纯化后的酶在银染SDS-PAGE中显示为单一条带。2. 天然分子量和亚基分子量分别为117 kDa和31 kDa。3. 动力学研究以及从抑制副产物获得的模式表明，该酶遵循有序的顺序动力学机制。4. 底物的降低的Km值有利于酶的活性。酶活性的“精细控制”由NADPH施加，其Ki比体内浓度低几倍。