Journal: Plants

Article Title: Evolutionary Implications of a Peroxidase with High Affinity for Cinnamyl Alcohols from Physcomitrium patens , a Non-Vascular Plant

doi: 10.3390/plants10071476

Figure Lengend Snippet: Purified PpaPrx19 is a strongly basic peroxidase. ( A ) Purification process of PpaPrx19, including adsorption chromatography on phenyl Sepharose (upper panel, peak F2) and cationic exchange chromatography on SP Sepharose (lower panel). Profiles of peroxidase activity and protein are denoted either by a continuous or by a dotted line, respectively. ( B ) Protein fingerprint in SDS-PAGE (left) and peroxidase isoenzyme pattern in IEF (right) of the crude extract (1) and the purified peroxidase (2) SDS-PAGE and IEF were revealed using the silver staining method and 4-MN in the presence of H 2 O 2 , respectively. ( C ) Dependence on pH of the purified PpaPrx19 activity. Data presented are average values ± SD of n = 3 experiments.

Article Snippet: In the first step, hydrophobic chromatography, proteins were separated on a phenyl Sepharose TM 6 Fast Flow (GE Healthcare, Barcelona, Spain) 31.5 × 1.0 cm gel bed column at a flow rate 1.0 mL·min −1 , and fractions of 5.0 mL were recovered.

Techniques: Purification, Adsorption, Chromatography, Activity Assay, SDS Page, Silver Staining

Journal: Plants

Article Title: Evolutionary Implications of a Peroxidase with High Affinity for Cinnamyl Alcohols from Physcomitrium patens , a Non-Vascular Plant

doi: 10.3390/plants10071476

Figure Lengend Snippet: Purification of basic peroxidase PpaPrx19 from P. patens . Peroxidase activity was measured using TMB as substrate.

Article Snippet: In the first step, hydrophobic chromatography, proteins were separated on a phenyl Sepharose TM 6 Fast Flow (GE Healthcare, Barcelona, Spain) 31.5 × 1.0 cm gel bed column at a flow rate 1.0 mL·min −1 , and fractions of 5.0 mL were recovered.

Techniques: Purification, Activity Assay, Protein Purification, Chromatography

Journal: PLoS ONE

Article Title: A Structural Domain Mediates Attachment of Ethanolamine Phosphoglycerol to Eukaryotic Elongation Factor 1A in Trypanosoma brucei

doi: 10.1371/journal.pone.0009486

Figure Lengend Snippet: (A), (B), T. brucei Δprocyclin#1 expressing HA-Alba-III and PTP-III fusion proteins were labeled with [ 3 H]Etn for 18 h. Proteins in the cell lysates (L), supernatants (SN), wash solutions (W) and immunoprecipitates (IP) were analyzed by SDS-PAGE using 12% acrylamide gels. SDS PAGE was followed either by immunoblotting (upper panels) or fluorography (lower panels). For immunoblotting α-HA antibody or α-IgG were used to detect HA-Alba-III or PTP-III, respectively. The lanes contain material from 1×10 7 parasites, except for the lanes with the immunoprecipitates in the fluorographs, which contain material prepared from 1.8×10 8 cell equivalents.

Article Snippet: The supernatant was supplemented with either anti-HA Affinity Matrix (Roche Diagnostics) or IgG Sepharose 6 Fast Flow matrix (GE Healthcare, Otelfingen, Switzerland) and incubated on a rotating device overnight at 4°C.

Techniques: Expressing, Labeling, SDS Page, Western Blot