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. 2011 Mar 31;7(3):333–346. doi: 10.7150/ijbs.7.333

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© Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.

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Fig 2 — Preliminary structure of native Gh-rTDH^WT protein. (A) Analytical ultracentrifugation determination of the Gh-rTDH^WT protein. The calculated molecular mass of Gh-rTDH^WT from sedimentation coefficient (s) is approximately 71,255.72 ± 10.83 g/mol. Plot of the distribution of sedimentation coefficients (c(s)) vs. S, where S is plotted in Svedberg units, calculated from the concentration profiles. (B) Gel filtration chromatography estimated molecular mass of Gh-rTDH^WT protein (open circle). The figure shows the migration positions of the Gh-rTDH^WT protein in comparison with the standard proteins used to calibrate the column. Closed diamonds indicate molecular mass standards: thyroglobulin (670 kDa), γ-globulin (158 kDa), albumin (66 kDa), ovalbumin (44 kDa), chymotrypsinogen A (25 kDa), myoglobulin (17 kDa), ribonuclease A (14 kDa). The inset shows the gel filtration analysis of Gh-rTDH^WT. (C) Representative electron microscopic image of negatively stained native form of Gh-rTDH^WT. The inset shows the image obtained by single-particle analysis.