Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Jun 7;13:903272. doi: 10.3389/fpls.2022.903272

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2022 Chen, Shen, Chou, Sato and Cheng.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

Protein N-glycosylation is altered in iU1 seedlings under salt stress. (A) Immunoblot analysis of N-glycoprotein profiles. The blots were hybridized with anti-HRP antibody or ConA (Concanavalin A, a jack bean lectin). Arrows indicate variations in band intensity between Col-0 and the iU1 lines under salt treatment. The cgl1-3 mutant proteins were loaded as an N-glycosylation control. (B,C) Immunoblot analyses reveal the change in the glycosylated state of PDI5 under 200 mM NaCl (B) or other salt concentration treatments (C). PNGase F and Endo H are enzymes that can remove N-glycan chains from glycoproteins and produce unglycosylated proteins. Total proteins were extracted from 14-day-old seedlings subjected to NaCl treatment. At least three independent experiments were performed in this study, and consistent results were obtained. Coomassie blue (CB) staining was used as a loading control.