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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

Adinolfi A, Hopkinson D A

Ann Hum Genet. 1979 Oct;43(2):109-19. doi: 10.1111/j.1469-1809.1979.tb02003.x.

The effects of coenzyme NAD and related compounds on the electrophoretic properties of the human ADH isozymes have been examined by the technique of affinity electrophoresis. 2. Incorporation of NAD, NADH or AMP into a starch-gel matrix leads to retardation in the cathodal mobilities of the gamma 2 gamma 2 and alpha alpha isozymes, but not the beta 1 beta 1 and gamma 1 gamma 1 isozymes. The heterodimeric isozymes show intermediate effects, and the genetic polymorphism at the ADH3 locus is only discernible if electrophoresis is carried out in the presence of coenzyme. 3. The behaviour of the ioszymes can be attributed to slight differences between the products (alpha, beta 1 and gamma 1) of the common alleles at the three ADH loci and a pronounced difference between the products (gamma 1 and gamma 2) of the alternative alleles at the ADH3 locus in their affinities for the cofactor NAD.

已通过亲和电泳技术研究了辅酶NAD及相关化合物对人乙醇脱氢酶同工酶电泳性质的影响。2. 将NAD、NADH或AMP掺入淀粉凝胶基质中会导致γ2γ2和αα同工酶的阴极迁移率降低，但β1β1和γ1γ1同工酶不受影响。异二聚体同工酶表现出中间效应，并且只有在辅酶存在下进行电泳时，才能辨别ADH3位点的遗传多态性。3. 同工酶的这种行为可归因于三个ADH位点常见等位基因的产物（α、β1和γ1）之间的细微差异，以及ADH3位点替代等位基因的产物（γ1和γ2）对辅因子NAD的亲和力存在显著差异。

Adinolfi A, Hopkinson D A

Ann Hum Genet. 1979 Oct;43(2):109-19. doi: 10.1111/j.1469-1809.1979.tb02003.x.

The effects of coenzyme NAD and related compounds on the electrophoretic properties of the human ADH isozymes have been examined by the technique of affinity electrophoresis. 2. Incorporation of NAD, NADH or AMP into a starch-gel matrix leads to retardation in the cathodal mobilities of the gamma 2 gamma 2 and alpha alpha isozymes, but not the beta 1 beta 1 and gamma 1 gamma 1 isozymes. The heterodimeric isozymes show intermediate effects, and the genetic polymorphism at the ADH3 locus is only discernible if electrophoresis is carried out in the presence of coenzyme. 3. The behaviour of the ioszymes can be attributed to slight differences between the products (alpha, beta 1 and gamma 1) of the common alleles at the three ADH loci and a pronounced difference between the products (gamma 1 and gamma 2) of the alternative alleles at the ADH3 locus in their affinities for the cofactor NAD.

已通过亲和电泳技术研究了辅酶NAD及相关化合物对人乙醇脱氢酶同工酶电泳性质的影响。2. 将NAD、NADH或AMP掺入淀粉凝胶基质中会导致γ2γ2和αα同工酶的阴极迁移率降低，但β1β1和γ1γ1同工酶不受影响。异二聚体同工酶表现出中间效应，并且只有在辅酶存在下进行电泳时，才能辨别ADH3位点的遗传多态性。3. 同工酶的这种行为可归因于三个ADH位点常见等位基因的产物（α、β1和γ1）之间的细微差异，以及ADH3位点替代等位基因的产物（γ1和γ2）对辅因子NAD的亲和力存在显著差异。