English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

1. Purified horse-liver alcohol dehydrogenase is heterogeneous on starch-gel electrophoresis in several buffer systems. 2. The electrophoretic pattern is altered by the addition to the buffers of oxidized or reduced coenzymes, isobutyramide, metal ions or metal-chelating agents. 3. The effect of coenzymes on the pattern suggests that the major cause of the observed heterogeneity is not the existence of isoenzymes, but the presence in the enzyme preparations of coenzyme-enzyme complexes or complexes with other nucleotides similar to, but less reactive than, the coenzymes. 4. Metal ions and chelating agents influence the electrophoretic separation by partial denaturation and inactivation of the enzyme.

Heterogeneity of liver alcohol dehydrogenase on starch-gel electrophoresis