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

Higher plant leaf protein was investigated for the enzyme activity catalyzing a thioredoxin-dependent reduction of 3'-phosphoadenylylsulphate (PAPS) to sulphite. The enzyme became detectable when heterologous thioredoxin from Escherichia coli was used substituting for the hitherto unidentified plant thioredoxin. The enzyme's cross-reactivity with heterologous thioredo­ xin enabled the partial purification and brief characterization. The molecular weight of the en­ zyme as estimated by HPLC size exclusion and gel filtration was 68-72 k. The protein reduced PAPS only when thioredoxin was present as cosubstrate. The function of this enzyme in the assimilation of inorganic sulphate by higher plants is discussed in comparison to the function of the respective enzymes from Escherichia coli and Saccharom yces cerevisiae.

Sulphate Assimilation in Higher Plants: A Thioredoxin-Dependent PAPS-Reductase from Spinach Leaves