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

. 2008 Nov 6;71(1):48–65. doi: 10.1111/j.1365-2958.2008.06508.x

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

Journal compilation © 2008 Blackwell Publishing

Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.

PMC Copyright notice

Fig. 1 — Production and characterization of the recombinant Pf332 DBL domain.

A. SDS-PAGE analysis of denatured Pf332 DBL domain solubilized from inclusion bodies then purified using NiNTA agarose. After the oxidative, in vitro refolding process, correctly refolded Pf332 DBL domain (AEX fractions #13 and #14) was separated from soluble multimers by anion-exchange chromatography (AEX). All samples shown in (A) were electrophoresed in sample buffer with (RD) or without (NR) reducing agent as indicated.

B. RP-HPLC analysis of the denatured starting material (SM) and the refolded Pf332 DBL domain (R). A decreased retention time is consistent with protein refolding. AUFS, Absorbance units full scale. C and D. Immunoblots for saponin-lysed P. falciparum 3D7 strain parasites were probed with (C) polyclonal mouse serum and (D) monoclonal antibody 10H2 each raised to the refolded Pf332 DBL domain. Parasite samples were electrophoresed with (RD) or without (NR) reducing agent in the sample buffer, then transferred onto PVDF membrane prior to commencing immunoblots.