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

The chickpea pathogenic fungus Ascochyta rabiei when growing in a pectin containing min­eral medium secretes an exo-polygalacturonase (PG) and a pectin methyl esterase into the cul­ture medium. The induction of the PG is controlled by catabolite repression. The PG was puri­fied to apparent homogeneity from the culture fluid by acetone precipitation and chromato­graphy on a Mono S and a Mono Q column. The molecular weight of the purified glycoprotein enzyme in SD S-PAGE was about 70 kDa, whereas the Mr by gelfiltration it was estimated to be 53 kDa. Polygalacturonic acid is the only substrate of the PG whereas pectin is not degraded. The PG releases only galacturonic acid from polygalacturonic acid and no oligogalacturonides which might elicitate chickpea plants and trigger plant defense response. The enzyme is not inhibited by pectin, the released proteins or phenolics.

Characterization of Pectic Enzymes from the Chickpea Pathogen Ascochyta rabiei