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

Phenylalanine ammonia-lyase (PAL) from the maize pathogen Ustilago maydis was analysed immunologically to obtain insights into the structural relationships between plant PAL and fungal PAL and between PAL and histidine ammonia-lyase (HAL). Cross-reactivity was found among all the PAL proteins from different species tested, using antibodies raised against both plant and fungal PALs. Both anti-Alfalfa and anti-popular PAL antibodies strongly recognized plant PALs but only weakly recognized fungal PALs. Antibodies raised against U. maydis PAL only weakly recognized the Rhodotorula glutinis yeast PAL. The anti-U. maydis PAL antibodies showed low affinity for the plant PALs but they bound strongly to Pseudomonas bacterial HAL. Significant cross-reactivity between the two plant PAL antibodies and the bacterial HAL was also observed. Both the anti-Ustilago PAL and the anti-poplar PAL antibodies displayed similar enzyme inhibition patterns, including moderate inhibition of bacterial HAL activity. However, the bacterial HAL antibody inhibited only Ustilago PAL. The PAL and HAL antibodies tested showed no inhibition against yeast PAL. This is first report on the immunological relationships between PAL and HAL.

Immunological Relationships among Fungal and Plant Phenylalanine Ammonia-lyases and Bacterial Histidine Ammonia-lyase