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

Human haemoglobin was prepared containing [14C]haem in either the alpha- or the beta-subunits. Coupled oxidation of such hybrid haemoglobins with ascorbate and O2 showed that the biliverdin produced by the alpha-subunits contained approx. 55% alpha-isomer and 45% beta-isomer, whereas that produced by the beta-subunits contained approx. 75% alpha-isomer and 25% beta-isomer. Coupled oxidation of isolated alpha- and beta-subunits gave approx. 70% alpha-isomer, 30% beta-isomer and 78% alpha-isomer, 22% beta-isomer respectively. These results are consistent with calculations of differences in the haem environment in the two subunit types.

Haem degradation in human haemoglobin in vitro. Separation of the contribution of the α- and β-subunits