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 Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

In a whole cell assay system with p-nitrophenyl phosphate as substrate, strains of Pseudomonas pseudomallei showed a two-peak pattern in pH activity curve of acid phosphatase, suggesting the presence of two enzyme components different in pH optimum (4.2 and 5.2). The component of 5.2 pH optimum was detected in the outer membrane fraction and the activity was resistant to heating at 70 C for 30 min. The other component of 4.2 pH optimum was heat-labile. No substantial difference was observed in the enzymatic activity between R and S type colonies.

HEAT-STABLE AND HEAT-LABILE COMPONENTS OF NON-SPECIFIC ACID PHOSPHATASE DETECTED IN PSEUDOMONAS PSEUDOMALLEI