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 smallest active form of aminopeptidase I (EC 3.4.11.1) from yeast has a molecular weight of 6.4 × 10 5 . At neutral pH the active enzyme is in equilibrium with two inactive subfragments (M r  = 3.2 × 10 5  and 1.1 × 10 5 ) as well as with higher aggregates (Mr ≧ 1.2 × 10 6 ). All of these species may be dissociated to give a single type of subunits with a molecular weight of 5.3 × 10 4 . It is concluded that the active enzyme is a dodecamer whereas the subfragments correspond to dimeric and hexameric forms.

The Quaternary Structure of Yeast Aminopeptidase I: 1. Molecular Forms and Subunit Size