<p>(A) Bis-tris−HEPES−MES buffer systems; (B) HEPES−Imidazole/Bis-tris buffer systems; (C) Imidazole−Acetic acid buffer systems. The PAGE was performed with a gradient resolving gel of 5%–20% in pH 7.0 and a stacking gel of 3% in pH 6.0, and 0.1% SDS was added in cathode buffers. The band patterns of each PAGE were visualized by Coomassie Blue G-250.</p
<p>(A) 12.5% SDS-PAGE. (B) 10% native-PAGE. (C) Activity staining of the bands in native-PAGE. M is ...
<p>(top left panel) SDS-PAGE with Coomassie staining and (remaining panels) size-exclusion chromatog...
<p>The gel disk of the low pI band (lane L) was cut out from the IEF gel rod and equilibrated in SDS...
<p>(A) Bis-tris−HEPES−MES buffer systems; (B) HEPES−Imidazole/Bis-tris buffer systems; (C) Imidazole...
<p>The PAGE with the stacking gel of 4% in pH 6.0 Bis-tris−HEPES−Acetic acid buffer was performed re...
<p>A and B. Coomasie blue stained gel. Lane M in A and B are protein molecular weight markers and th...
<p>The PAGE was carried out with a resolving gel of 9% in pH 6.5 Bis-tris−HEPES−MES buffer and with ...
<p>(A) Coomassie brilliant blue staining of SDS PAGE gel. The first and last lanes correspond to the...
<p>Proteins (∼2 µg per lane) were reduced with 5% BME or loaded on a 12% gel in non-reducing conditi...
<p>(A) the Tris−Gly PAGE with a resolving gel of 6.5% in pH 8.8 Tris−HCl buffer, a staking gel of 3%...
<p>A) Native PAGE analysis of BS<sup>3</sup> conjugated pC1-inh (lane 1), pC1-inh (lane 2) and nativ...
<p>A. Purity and protein molecular weight were visualised by SDS-PAGE in a 12.5% polyacrylamide gel ...
<p>The same gel was first stained with Coomassie Brilliant Blue (CBB, left) and then with silver (ri...
<p>The 2D gel resolved by isoelectricfocusing in the first dimension (pH range 3–10) followed by SDS...
<p>(a) Total protein from whole virions or proteinase K (ProK) treated virions was separated by 1D-S...
<p>(A) 12.5% SDS-PAGE. (B) 10% native-PAGE. (C) Activity staining of the bands in native-PAGE. M is ...
<p>(top left panel) SDS-PAGE with Coomassie staining and (remaining panels) size-exclusion chromatog...
<p>The gel disk of the low pI band (lane L) was cut out from the IEF gel rod and equilibrated in SDS...
<p>(A) Bis-tris−HEPES−MES buffer systems; (B) HEPES−Imidazole/Bis-tris buffer systems; (C) Imidazole...
<p>The PAGE with the stacking gel of 4% in pH 6.0 Bis-tris−HEPES−Acetic acid buffer was performed re...
<p>A and B. Coomasie blue stained gel. Lane M in A and B are protein molecular weight markers and th...
<p>The PAGE was carried out with a resolving gel of 9% in pH 6.5 Bis-tris−HEPES−MES buffer and with ...
<p>(A) Coomassie brilliant blue staining of SDS PAGE gel. The first and last lanes correspond to the...
<p>Proteins (∼2 µg per lane) were reduced with 5% BME or loaded on a 12% gel in non-reducing conditi...
<p>(A) the Tris−Gly PAGE with a resolving gel of 6.5% in pH 8.8 Tris−HCl buffer, a staking gel of 3%...
<p>A) Native PAGE analysis of BS<sup>3</sup> conjugated pC1-inh (lane 1), pC1-inh (lane 2) and nativ...
<p>A. Purity and protein molecular weight were visualised by SDS-PAGE in a 12.5% polyacrylamide gel ...
<p>The same gel was first stained with Coomassie Brilliant Blue (CBB, left) and then with silver (ri...
<p>The 2D gel resolved by isoelectricfocusing in the first dimension (pH range 3–10) followed by SDS...
<p>(a) Total protein from whole virions or proteinase K (ProK) treated virions was separated by 1D-S...
<p>(A) 12.5% SDS-PAGE. (B) 10% native-PAGE. (C) Activity staining of the bands in native-PAGE. M is ...
<p>(top left panel) SDS-PAGE with Coomassie staining and (remaining panels) size-exclusion chromatog...
<p>The gel disk of the low pI band (lane L) was cut out from the IEF gel rod and equilibrated in SDS...