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

A systematic study of the homologous series of omega-aminoalkyl-agaroses revealed differences in the affinities of 6-hydroxy-D- and 6-hydroxy-L-nicotine oxidase. In contrast to supports with nonpolar alkyl chains, omega-aminoalkyl-agarose showed high affinity towards the L-specific enzyme, while the D-specific oxidase was bound most firmly by omega-aminododecyl-agarose. 6-Hydroxy-L-nicotine oxidase could be desorbed by 1.3M NaCl only in the presence of the substrate L-6-hydroxynicotine. Using the omega-aminoalkyl-agarose, a complete separation of the enantiozymes was accomplished and an efficient purification procedure for both oxidases established.

Purification of the Flavoproteins 6-Hydroxy-D- and 6-Hydroxy-L-nicotine Oxidase Using Hydrophobic Affinity Chromatography