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Figure 1 | BMC Biotechnology

Figure 1

From: Heterologous expression and biochemical characterization of a highly active and stable chloroplastic CuZn-superoxide dismutase from Pisum sativum

Figure 1

Molecular mass of purified PschSOD and spectral analysis. (A) Native molecular mass of recombinant PschSOD was measured with respect to standard protein marker as resolved in Biosil-250 analytical gel filtration column. Standard proteins used were: (a) 160 kDa-Glucose oxidase (b) 66.5 kDa-BSA fraction V (c) 29 kDa-Carbonic anhydrase and (d) 16 kDa-Bovine CuZn SOD (monomer) respectively (B). The 15% SDS–PAGE showing PschSOD subunit. Subunit molecular mass as calculated using the molecular standard markers (M)suggest that the subunit mass of the protein is ~ 18 kDa.Western blot taking1μg of the protein and probed with poly-his antibody has been shown in (C) while probed using CuZn-SOD specific antibody has been depicted in (D). (E) Room temperature (25°C) UV-Visible electronic transition spectra of 2 mg ml−1 PschSOD. The inset depicts the spectral resolution in an extended scale showing prominent broad peak at 670 nm, characteristics of d-d transition for copper in CuZn-SODs. CD spectral analysis of the protein at 25°C is represented in (F). Negative band at 208 nm region and positive band at 196 nm is shown which suggest abundance of β-sheet in the protein.

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BMC Biotechnology

ISSN: 1472-6750

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