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/

Zendy Plus

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

Zendy Tools

Zendy Open

The malate dehydrogenase activity in the cytosolic fraction isolated from chicken hepatocytes is resolved by DEAE-Sephacel chromatography in three active, electrophoretically distinct, species obtained in homogeneous form by affinity chromatography on 5'-AMP-Sepharose and Blue-Sepharose. Two of those species, according to the results obtained, might represent different conformational isomers of the enzyme molecule. Their purified preparations show identical amino-acid compositions and physico-chemical properties very similar to those of the cytosolic isoenzyme of other sources. The third one corresponds to a slight contamination of the mitochondrial isoenzyme.

Malate Dehydrogenase Species in the Cytosolic Fraction of Chicken Liver