<p>(a) The gel stained with Coomassie Brilliant Blue R-250. Lane M: protein marker; Lane 1: purified LacTT after heat denaturation; Lane 2: purified LacTT without heat denaturation. (b) The zymogram stained with 0.1 mM SGZ and 2 mM guaiacol. Lane M: protein marker; Lane 1: unheated purified LacTT stained with 0.1 mM SGZ; Lane 2: unheated purified LacTT stained with 2 mM guaiacol; Lane 3: heat-denatured LacTT stained with 0.1 mM SGZ; Lane 4: heat-denatured LacTT stained with 2 mM guaiacol. (c) Deglycosylation analyses of the purified laccase. Lane 1: purified LacTT; Lane 2: purified LacTT was deglycosylated by PNGase F; Lane M: protein marker.</p
<p>The gel was stained with Coomassie Blue. Lane 1: EZ-Run protein molecular weight marker (170, 130...
<p>After electrophoresis, the gel was visualized by Coomassie brilliant blue R250 staining. Lane 1: ...
<p>(A). SDS-PAGE of RKOD with or without digestion with Endo H. M, protein molecular weight marker (...
<p>(a) Lane 1: denatured protein marker, Lane 2: purified laccase; (b) Lane 1: purified laccase with...
<p>(A) Heated laccases were separated and visualized by coomassie brilliant blue (CBR) staining and ...
<p>The purified proteins were separated on a 12.5% gel under reducing or non-reducing conditions: (A...
<p>A: M, Protein markers, lane 1, purified Lac3, lane 2, endoglycosidase-H-treated Lac3; B: M, Prote...
<p>SDS-PAGE analysis of the purified recombinant Xyl3A. Lanes: 1, the purified recombinant Xyl3A aft...
<p>A: The glycoprotein staining experiment. Lane 1: BSA; Lane2: purified glycosylated keratinase. B:...
<p>Lane 1, whole-cell extract from non-induced cells; lane 2, whole-cell extract from post-induction...
<p>The zymogram process was carried out using native PAGE, and the enzyme band was visualized by inc...
<p>Gels were stained with Coomassie Blue R. Arrows indicate the purified proteins. MW, molecular wei...
<p>(A) Time course of laccase activity and secreted protein levels produced by <i>Cerrena</i> sp. HY...
<p>(Protein samples were denatured by heating for 5 min in the presence of SDS and β-mercaptoethanol...
<p>Molecular weight determination of purified enzyme (a) SDS PAGE for steps of purifying L-asparagin...
<p>The gel was stained with Coomassie Blue. Lane 1: EZ-Run protein molecular weight marker (170, 130...
<p>After electrophoresis, the gel was visualized by Coomassie brilliant blue R250 staining. Lane 1: ...
<p>(A). SDS-PAGE of RKOD with or without digestion with Endo H. M, protein molecular weight marker (...
<p>(a) Lane 1: denatured protein marker, Lane 2: purified laccase; (b) Lane 1: purified laccase with...
<p>(A) Heated laccases were separated and visualized by coomassie brilliant blue (CBR) staining and ...
<p>The purified proteins were separated on a 12.5% gel under reducing or non-reducing conditions: (A...
<p>A: M, Protein markers, lane 1, purified Lac3, lane 2, endoglycosidase-H-treated Lac3; B: M, Prote...
<p>SDS-PAGE analysis of the purified recombinant Xyl3A. Lanes: 1, the purified recombinant Xyl3A aft...
<p>A: The glycoprotein staining experiment. Lane 1: BSA; Lane2: purified glycosylated keratinase. B:...
<p>Lane 1, whole-cell extract from non-induced cells; lane 2, whole-cell extract from post-induction...
<p>The zymogram process was carried out using native PAGE, and the enzyme band was visualized by inc...
<p>Gels were stained with Coomassie Blue R. Arrows indicate the purified proteins. MW, molecular wei...
<p>(A) Time course of laccase activity and secreted protein levels produced by <i>Cerrena</i> sp. HY...
<p>(Protein samples were denatured by heating for 5 min in the presence of SDS and β-mercaptoethanol...
<p>Molecular weight determination of purified enzyme (a) SDS PAGE for steps of purifying L-asparagin...
<p>The gel was stained with Coomassie Blue. Lane 1: EZ-Run protein molecular weight marker (170, 130...
<p>After electrophoresis, the gel was visualized by Coomassie brilliant blue R250 staining. Lane 1: ...
<p>(A). SDS-PAGE of RKOD with or without digestion with Endo H. M, protein molecular weight marker (...