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

As shown previously, during degradation of sucrase-isomaltase in rat jejunum, degradation of the sucrase active site occurs before that of isomaltase active site [Goda &amp; Koldovský (1985) Biochem. J. 229, 751-758]. To characterize further the process of sucrase-isomaltase degradation in jejunum, we determined the amounts of immunoreactive sucrase-isomaltase in rat jejunum by using a monoclonal-antibody-based enzyme-linked immunosorbent assay. By employing two alternative monoclonal antibodies (one reacting with the sucrase subunit and the other reacting with the isomaltase subunit), the amount of antigen-containing sucrase subunit and the amount of antigen-containing isomaltase subunit were separately quantified. In both upper and lower jejunum of rats, the amount of antigen-containing isomaltase subunit was always higher than the amount of antigen-containing sucrase subunit. This difference was attributable mainly to a degradation product of sucrase-isomaltase, which was identified as isomaltase monomer. Occlusion of pancreatic ducts for 18 h eliminated the difference between the amount of antigen-containing sucrase subunit and the amount of antigen-containing isomaltase subunit in both upper and lower jejunum. In jejunum of control animals, the molar ratio of sucrase subunit to isomaltase subunit was estimated to be 0.32-0.52, indicating that quite a large proportion of sucrase-isomaltase (48-68%) is present as degradation products (e.g. isomaltase monomer). These results support the model of degradation process of sucrase-isomaltase in brush-border membranes of rat jejunum, whereby degradation of sucrase subunit by the action of pancreatic proteinase(s) precedes degradation of isomaltase subunit.

Characterization of degradation process of sucrase-isomaltase in rat jejunum with monoclonal-antibody-based enzyme-linked immunosorbent assay