<p>The enzyme was run in parallel with molecular mass standards on a 12% gel and stained with Coomassie Blue R-250. Lane 1: molecular mass markers (97, 66, 45, 31, 21.3 and 14.4 kDa). Lanes 2 and 5: empty lanes. Lane 3 and 4: 250 mM ImOH Nichel fractions. Lane 6: gel filtration, pooled fractions.</p
<p>Proteins (∼2 µg per lane) were reduced with 5% BME or loaded on a 12% gel in non-reducing conditi...
<p>Lane 1, PNGase F-treated RhaL1; Lane 2, purified recombinant RhaL1; M, molecular mass markers.</p
<p>All proteins were loaded at a concentration of 2–10 µM on the gel filtration column. Dilution dur...
<p>Steady state kinetics of recombinant HpASNase wild type and variants as a function of L-ASN (pane...
<p>Plots of the residual activities at 10 min incubation <i>vs.</i> temperature. The enzyme solution...
<p>From left to right, every three consecutive lanes represent a protein, and the protein name is gi...
<p>A. Purified and refolded pro-enzymes of mutants and wild-type were analyzed in 15% SDS-PAGE; M de...
<p>(A) Coomassie brilliant blue staining of SDS PAGE gel. The first and last lanes correspond to the...
<p>(A) Fractions are shown for the different purification steps of wild-type 4-HPPD. Lane 1, cell cr...
<p>Near-homogeneous fractions (∼2 µg) of recombinant <i>Hs</i>mtSSBwt (<i>lane 1</i>), ΔN (<i>lane 2...
<p>Lanes were loaded with 1.75 μg per lane. M: molecular weight markers, A: pp-dPA83 (<i>in vivo</i>...
<p>Lane 1: protein standard; Lane 2: R18; Lane 3: R43. Powdered enzyme (100 µg) was dissolved in dis...
<p>All gels were loaded in the same manner. Lane 1: Dual color protein ladder (BioRad, Hercules, CA)...
<p>(A) Bis-tris−HEPES−MES buffer systems; (B) HEPES−Imidazole/Bis-tris buffer systems; (C) Imidazole...
<p>12% SDS-PAGE gel of the purified protein of hAS3MT mutants were stained with Coomassie blue.</p
<p>Proteins (∼2 µg per lane) were reduced with 5% BME or loaded on a 12% gel in non-reducing conditi...
<p>Lane 1, PNGase F-treated RhaL1; Lane 2, purified recombinant RhaL1; M, molecular mass markers.</p
<p>All proteins were loaded at a concentration of 2–10 µM on the gel filtration column. Dilution dur...
<p>Steady state kinetics of recombinant HpASNase wild type and variants as a function of L-ASN (pane...
<p>Plots of the residual activities at 10 min incubation <i>vs.</i> temperature. The enzyme solution...
<p>From left to right, every three consecutive lanes represent a protein, and the protein name is gi...
<p>A. Purified and refolded pro-enzymes of mutants and wild-type were analyzed in 15% SDS-PAGE; M de...
<p>(A) Coomassie brilliant blue staining of SDS PAGE gel. The first and last lanes correspond to the...
<p>(A) Fractions are shown for the different purification steps of wild-type 4-HPPD. Lane 1, cell cr...
<p>Near-homogeneous fractions (∼2 µg) of recombinant <i>Hs</i>mtSSBwt (<i>lane 1</i>), ΔN (<i>lane 2...
<p>Lanes were loaded with 1.75 μg per lane. M: molecular weight markers, A: pp-dPA83 (<i>in vivo</i>...
<p>Lane 1: protein standard; Lane 2: R18; Lane 3: R43. Powdered enzyme (100 µg) was dissolved in dis...
<p>All gels were loaded in the same manner. Lane 1: Dual color protein ladder (BioRad, Hercules, CA)...
<p>(A) Bis-tris−HEPES−MES buffer systems; (B) HEPES−Imidazole/Bis-tris buffer systems; (C) Imidazole...
<p>12% SDS-PAGE gel of the purified protein of hAS3MT mutants were stained with Coomassie blue.</p
<p>Proteins (∼2 µg per lane) were reduced with 5% BME or loaded on a 12% gel in non-reducing conditi...
<p>Lane 1, PNGase F-treated RhaL1; Lane 2, purified recombinant RhaL1; M, molecular mass markers.</p
<p>All proteins were loaded at a concentration of 2–10 µM on the gel filtration column. Dilution dur...