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

The mutantam-14 produces no active nicotinamide adenine dinucleotide phosphate-linked glutamate dehydrogenase (GDH) and no protein showing immunological cross-reaction with the enzyme. Nevertheless, it shows complementation with several otheram mutants in heterokaryons. Active GDH can be extracted from heterokaryons formed fromam-14 and other mutants which, by themselves, produce more or less inactive varieties of the enzyme. The enzyme fromam-14 +am-3 heterokaryons can be partially separated fromam-3 mutant GDH on a diethylaminoethyl cellulose column. It is characterized by abnormally high thermolability and by a capacity for activation by glutamate. By the same procedure as brings about hybridization between mutant GDH proteins, it has been possible to recover enzyme with the properties of puream-3 GDH from a partially purifiedam-14 +am-3 GDH preparation which was initially substantially free of unhybridizedam-3 enzyme. This is interpreted as evidence that the active complementation product is a hybrid oligomer containingam-3 monomers and alsoam-14 monomers, the latter being unable to aggregate by themselves. Heterokaryons formed fromam-14 and wild type produce GDH of abnormally high thermolability, presumably due to the formation ofam-14 +am + hybrids.

Nature of the Complementation Products Formed by a Complementing Mutant of Neurospora crassa