Published April 30, 2015 | Version v1
Figure Open

Fig. 5 in Identification of the pI 4.6 extensin peroxidase from Lycopersicon esculentum using proteomics and reverse-genomics

Description

Fig. 5. In vitro crosslinking assays using tomato P1 extensin. Extensin crosslinking assays (30 min) were performed using tomato P1 extensin substrate to test the activities of folded CG5-6xHis. Control assays included folding solution (A), water (B), corresponding proteins isolated from E. coli transformed with the empty vector-EV (C), and horseradish peroxidase (D). Extensin polymerization was observed when either CG5-6xHis (E) or the tomato pI 4.6 EP (F) was added. Crosslinking is observed by the size shift in P1 monomer by gel permeation chromatography upon forming P1 oligomer and P1 polymer with concomitant decrease in P1 monomer. Extended incubation times leave much of the P1 polymer formed in (E) and (F) insoluble (e.g. not detected by gel-filtration).

Notes

Published as part of Dong, Wen, Kieliszewski, Marcia & Held, Michael A., 2015, Identification of the pI 4.6 extensin peroxidase from Lycopersicon esculentum using proteomics and reverse-genomics, pp. 151-159 in Phytochemistry 112 (1) on page 155, DOI: 10.1016/j.phytochem.2014.09.015, http://zenodo.org/record/10487683

Files

figure.png

Files (256.6 kB)

Name Size Download all
md5:61ca7954723f2a4541d38bc99b8317e7
256.6 kB Preview Download

Linked records

Additional details

Related works

Is part of
Journal article: 10.1016/j.phytochem.2014.09.015 (DOI)
Journal article: urn:lsid:plazi.org:pub:E77AFFC1FFE20543BD1E57660B4F4554 (LSID)
Journal article: https://zenodo.org/record/10487683 (URL)