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

Summary: Chloramphenicol acetyl transferase (CAT) was purified from Escherichia coli K12 carrying R1 and 222 and from E. coli K12 recA (R1 Cm87/R100-99 TcRCmS). The third enzyme has a lower affinity for chloramphenicol and greater heat lability than those specified by R1 and 222, compatible with the enzyme's resulting from interallelic complementation. CAT has a molecular weight of 80000, with subunits of 20000. Material cross reacting with anti-222 CAT serum was detected in CmS mutant cell sonicates.

Chloramphenicol Acetyl Transferase Formed by Wild-type and Complementing R Factors in Escherichia coli K12