1,721,616 research outputs found
Analysis of HLA-B27 HC by Endo H digestion.
No full text<p>(A) SDS-PAGE analysis of Endo H-resistant and Endo H-sensitive HLA-B27 HC in C1R-B2704 cells. C1R-B2704 cells were treated with the indicated reagents. Membrane proteins (2 μg) digested with Endo H (one unit) were analyzed by reducing SDS-PAGE and immunoblotted by BH2 monoclonal antibody. (B) The results obtained in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0077451#pone-0077451-g005" target="_blank">Figure 5A</a> were plotted. The ratio of Endo H-sensitive HLA-B27 HC/total HLA-B27 HC is averaged from three independent experiments (mean ± SD, n =3).</p
The hydrolytic activity of Endo H-P to proteins from mammals and baker's yeast.
No full text<p>(A). The hydrolytic activity of Endo H-P to EPO expressed in CHO cells. Lane 1 EPO without treatment; Lane 2 EPO treated with commercial Endo H; Lane 3 EPO treated with purified Endo H-P; Lane 4 EPO treated with commercial PNGase F. (B). The hydrolytic activity of Endo H-P to CPY from baker's yeast. Lane 1 CPY without treatment; Lane 2 CPY treated with commercial Endo H; Lane 3 CPY treated with purified Endo H-P.</p
The alignments of <i>Endo H-P</i> with wild-type <i>Endo H</i>.
No full text<p>The nucleotide sequence of <i>Endo</i> H-<i>P</i> was compared with that of wild-type <i>Endo</i> H, the result indicated that 220 nucleotides were altered in <i>Endo H-P</i>.</p
Endo H sensitivity and deglycosylation studies of CLN5.
No full text<p>(A) Whole cell lysates transiently expressing N-glycosylation mutants were digested with Endo H enzyme and analyzed by Western blotting. (B) Western blotting of uncut, Endo H, or PNGase F treated whole cell lysates expressing wt CLN5, as well as whole cell lysates from CLN5 transfection in the presence of tunicamycin. Equal amount of lysates was loaded onto each well. The mouse monoclonal anti-Myc antibody was used to detect CLN5.</p
Western blot analysis of rhIGFBP-3 digested by Endo H in transgenic rice seeds.
No full text<p>Total protein was extracted from mature dehulled seeds of SB-57 and SBK-66 transgenic lines and digested by Endo H. Lane 1: SB-57; lane 2: SB-57 digested by Endo H; lane 3: marker; lane 4: SBK-66; and lane 5: SBK-66 digested by Endo H.</p
Analyzing the characteristics of Endo H-P through mobility shift assay of RNase B.
No full text<p>(A).Identifying the optimum temperature of Endo H-P with SDS-PAGE. M protein molecular weight markers (the size of each band was indicated on the left);Lane 1 to Lane 6 denatured RNase B treated with concentrated Endo H-P at 25°C, 30°C, 35°C, 40°C, 45°C and 50°C, respectively; Lane 7 denatured RNase B treated with concentrated Endo H-P at 37°C, respectively;Lane 8 the negative control (RNase B without treatment); Lane 9 the positive control (overdose of Endo H-P was added to the reaction system);(B). Identifying the optimum temperature of Endo H-P with SDS-PAGE. M protein molecular weight markers (the size of each band was indicated on the left);Lane 1 the positive control (overdose of Endo H-P was added to the reaction system); Lane 2 the negative control (RNase B without treatment);Lane 3–8 denatured RNase B treated with Endo H-P at pH5.0, 5.5, 6.0, 6.5, 7.0 and 7.5, respectively.</p
The content of mannose rich (endo H sensitive) synaptophysin in retinas from diabetic and control rats.
No full text<p>Retinal lysates were treated with endo H to quantify mannose rich glycosylated synaptophysin. A) Endo H treated samples from 1-month STZ-diabetic rats and controls had an additional band at 35 kDa below the 38 kDa synaptophysin band. B) There was a significantly more endo H-sensitive synaptophysin in the retinal lysates from 1-month STZ-diabetic rats compared to age-matched controls (<i>n</i> = 8; *<i>p</i><0.05). C) Endo H treated samples from 2-month STZ-diabetic rats and controls also had an additional band at 35 kDa below the 38 kDa synaptophysin band. D) There was no significant difference in endo H-sensitive synaptophysin between retinal lysates from 2-month STZ-diabetic rats compared to age-matched controls (<i>n</i> = 8).</p
Determining the enzyme activity of Endo H-P through mobility shift assay of RNase B.
No full text<p>M protein molecular weight markers (the size of each band was indicated on the left); Lane 1 denatured RNase B (negative control); Lane 2 denatured RNase B treated with 1 U of commercial Endo H from NEB, USA (positive control); Lane 3–8 denatured RNase B treated with 1μl of Endo H-P diluted into 5.0%, 4.0%, 3.5%, 3.0%, 2.5% and 2.0%, respectively.</p
Prediction of thermal stratification in a u-bent pipe: A URANS validation
Full text linkIn the present study, CFD is employed to investigate phenomena occurring during a process of thermal stratification in U-bent pipes at transitional Reynolds number. URANS evaluation had been chosen for its low computational costs during transient analysis and for the evaluation of modeling performance in these conditions. Application of CFD at transitional Reynolds number and buoyancy driven flows indeed contains deeper uncertainties in relation to the range of applicability for hydrodynamic and thermal models. The methodology applied in the work points out, through validations with the basic problems constituting the complex stratified phenomenon, the applicability of the current turbulence modeling. Accurate predictions have been found in relation to transitional Reynolds number in bent pipes and region of stability induced by the gravitational field. On the other hand the defects introduced in the unstable region of the U bent pipe, are discussed in relation to the adopted modeling
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