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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

Auricchio F, Bruni C B, Sica V

Biochem J. 1968 Jun;108(2):161-7. doi: 10.1042/bj1080161.

Centrifugation of rat liver acid glucosidase, which had been purified by adsorption on dextran gel, on a density gradient of sucrose showed the enzyme to be impure. 2. Preliminary purification of the enzyme before the gel filtration improved the final degree of purity of this preparation. Disc gel electrophoresis of this preparation showed a single band of protein. 3. The sedimentation co-efficient and the molecular weight determined on a sucrose gradient were 4.9-5.1s and 76000-83000 respectively for the rat liver enzyme, and 5.6s and 97000 for the acid alpha-glucosidase purified by means of the same procedure from the human kidney. 4. The Michaelis constants of rat liver and human kidney enzyme were 4.7x10(-3)m and 13.6x10(-3)m respectively with maltose as substrate. 5. The enzyme from both tissues was inhibited by tris and by erythritol. The inhibition of the rat liver acid glucosidase by erythritol was competitive.

用葡聚糖凝胶吸附法纯化的大鼠肝脏酸性葡萄糖苷酶在蔗糖密度梯度上离心，结果显示该酶不纯。2. 在凝胶过滤之前对该酶进行初步纯化提高了此制剂的最终纯度。对此制剂进行圆盘凝胶电泳显示出一条单一的蛋白质带。3. 对于大鼠肝脏酶，在蔗糖梯度上测定的沉降系数和分子量分别为4.9 - 5.1s和76000 - 83000，而通过相同程序从人肾纯化的酸性α-葡萄糖苷酶的沉降系数和分子量分别为5.6s和97000。4. 以麦芽糖为底物时，大鼠肝脏酶和人肾酶的米氏常数分别为4.7×10⁻³m和13.6×10⁻³m。5. 来自这两种组织的酶都受到三羟甲基氨基甲烷（tris）和赤藓醇的抑制。赤藓醇对大鼠肝脏酸性葡萄糖苷酶的抑制是竞争性的。

Auricchio F, Bruni C B, Sica V

Biochem J. 1968 Jun;108(2):161-7. doi: 10.1042/bj1080161.

Centrifugation of rat liver acid glucosidase, which had been purified by adsorption on dextran gel, on a density gradient of sucrose showed the enzyme to be impure. 2. Preliminary purification of the enzyme before the gel filtration improved the final degree of purity of this preparation. Disc gel electrophoresis of this preparation showed a single band of protein. 3. The sedimentation co-efficient and the molecular weight determined on a sucrose gradient were 4.9-5.1s and 76000-83000 respectively for the rat liver enzyme, and 5.6s and 97000 for the acid alpha-glucosidase purified by means of the same procedure from the human kidney. 4. The Michaelis constants of rat liver and human kidney enzyme were 4.7x10(-3)m and 13.6x10(-3)m respectively with maltose as substrate. 5. The enzyme from both tissues was inhibited by tris and by erythritol. The inhibition of the rat liver acid glucosidase by erythritol was competitive.

用葡聚糖凝胶吸附法纯化的大鼠肝脏酸性葡萄糖苷酶在蔗糖密度梯度上离心，结果显示该酶不纯。2. 在凝胶过滤之前对该酶进行初步纯化提高了此制剂的最终纯度。对此制剂进行圆盘凝胶电泳显示出一条单一的蛋白质带。3. 对于大鼠肝脏酶，在蔗糖梯度上测定的沉降系数和分子量分别为4.9 - 5.1s和76000 - 83000，而通过相同程序从人肾纯化的酸性α-葡萄糖苷酶的沉降系数和分子量分别为5.6s和97000。4. 以麦芽糖为底物时，大鼠肝脏酶和人肾酶的米氏常数分别为4.7×10⁻³m和13.6×10⁻³m。5. 来自这两种组织的酶都受到三羟甲基氨基甲烷（tris）和赤藓醇的抑制。赤藓醇对大鼠肝脏酸性葡萄糖苷酶的抑制是竞争性的。