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

. 2017 Jun 1;174(3):1807–1824. doi: 10.1104/pp.17.00401

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

© 2017 American Society of Plant Biologists. All Rights Reserved.

PMC Copyright notice

Figure 8. — Characterization of HCF222. A, Immunodetection of HCF222-HA in leaf extracts. After SDS-PAGE, the protein pattern of whole-leaf extracts (Leaf) and whole-leaf membrane (M) and soluble fraction (S) from wild-type (WT) and complemented plants was transferred to nitrocellulose, and the fusion protein was detected with anti-HA antibody. B, Measurement of disulfide reductase activity of recombinant HCF222-6xHis by the reductive insulin assay. The reduction of disulfide bonds in insulin was monitored by an increase in A₆₅₀, which results from insulin precipitation. The concentration of recombinant HCF222-6xHis was estimated after SDS-PAGE and Coomassie Blue staining in comparison with a dilution series of lysozyme. DTT without enzyme served as a control. In addition, recombinant β-galactosidase-6xHis from similarly purified E. coli extracts served as a negative control to estimate contaminants from E. coli. Values represent means of three independent experiments, each with three replicates; β-galactosidase activity is shown as means of three replicates from one purification. Means with sd are depicted.