Journal: European journal of biochemistry

Article Title: The N-glycans of jack bean alpha-mannosidase. Structure, topology and function.

doi: 10.1046/j.1432-1327.1999.00598.x

Figure Lengend Snippet: Fig. 1. HPLC profiles of PA-sugar chains from jack bean a-man- nosidase. Panel A: RP-HPLC of PA-derivatives from jack bean a-man- nosidase. The PA-derivatives were applied onto a Cosmosil 5C18-AR (6.0 250 mm) column and eluted as described in the text. The run- through-fraction (around 9 min) contained some PA-derivatives bearing only one GlcNAc residue at their reducing-ends, which are known to be derived from released intact N-glycans as by-products of hydrazinolysis [7,12]. Panel B: Size-fractionation HPLC of the partially purified PA-sugar chains shown in Panel A (Peaks I and II) by RP-HPLC.

Article Snippet: The two glycopeptide fractions [elution volume from 244±292 mL (high-mannose-type glycan) and from 408±500 mL (complex-type glycan)] were concentrated in a rotary evaporator and the former glycopeptide-fraction was applied to a Jasco 880-PU HPLC apparatus with a Poros R1 column (4.6 100 mm).

Techniques: Residue, Derivative Assay, Fractionation, Purification

Journal: European journal of biochemistry

Article Title: The N-glycans of jack bean alpha-mannosidase. Structure, topology and function.

doi: 10.1046/j.1432-1327.1999.00598.x

Figure Lengend Snippet: Fig. 3. RP-HPLC of a lysylendopeptidase digest of alkylated jack bean a-mannosidase. The lysylendopeptidase digest of alkylated jack bean a- mannosidase (100 mg) was applied onto a Vydac C8 column. The column was eluted by a linear gradient of 2±40% acetonitrile in 0.1% trifluoroacetic acid. Panel A: Total ion monitoring chromatogram (TIC). `RT: 28.2 min' indicates the position of glycopeptide (GP) which eluted after 28.2 min. Panel B: Precursor ion (m/z 366.0; Hex-HexNAc) monitoring. Panel C: Precursor ion (m/z 204.1; HexNAc) monitoring. Panel D: ESI-MS spectrum of the glycopeptide GP (complex-type) from Panel A.

Article Snippet: The two glycopeptide fractions [elution volume from 244±292 mL (high-mannose-type glycan) and from 408±500 mL (complex-type glycan)] were concentrated in a rotary evaporator and the former glycopeptide-fraction was applied to a Jasco 880-PU HPLC apparatus with a Poros R1 column (4.6 100 mm).

Techniques: Glycoproteomics

Journal: European journal of biochemistry

Article Title: The N-glycans of jack bean alpha-mannosidase. Structure, topology and function.

doi: 10.1046/j.1432-1327.1999.00598.x

Figure Lengend Snippet: Fig. 5. RP-HPLC of a glycopeptide-fraction obtained by gel-filtration of a lysylendopeptidase-digest of alkylated jack bean a-mannosidase. The glycopeptide fraction obtained by Sephadex G-25 gel-filtration (fraction volume from 244 to 292 mL) was applied onto a Poros R1 column. The column was eluted with 5% acetonitrile in 0.1% trifluoroacetic acid for 5 min, followed by a linear gradient of 5±60% acetonitrile in 0.1% trifluoroacetic acid. Only the peak indicated by an arrow was found to contain neutral sugars. GP (high-mannose-type) indicates a glycopeptide bearing the high-mannose-type N-glycan.

Article Snippet: The two glycopeptide fractions [elution volume from 244±292 mL (high-mannose-type glycan) and from 408±500 mL (complex-type glycan)] were concentrated in a rotary evaporator and the former glycopeptide-fraction was applied to a Jasco 880-PU HPLC apparatus with a Poros R1 column (4.6 100 mm).

Techniques: Glycoproteomics, Filtration

Journal: BMC pulmonary medicine

Article Title: IL-32 induces epithelial-mesenchymal transition by triggering endoplasmic reticulum stress in A549 cells.

doi: 10.1186/s12890-020-01319-z

Figure Lengend Snippet: Fig. 4 GRP78 expression characteristics induced by IL-32 or 4-PBA. a GRP78 mRNA expression levels. *P < 0.05 compared with the control group, **P < 0.05 compared with the rhIL-32 group. b and c GRP78 protein expression levels, measured by western blotting. *P < 0.05 compared with the control group, **P < 0.05 compared with the rhIL-32 group

Article Snippet: A sample containing 20 μg of protein was separated on a 12% sodium dodecyl sulfate-polyacrylamide gel electrophoresis gel (Solarbio), transferred to a polyvinylidene fluoride membrane, and incubated with rabbit anti-mouse N-cadherin, GRP78, and α-SMA primary antibodies (Proteintech, Wuhan, China), or βactin antibody (Bioss, Beijing, China) as a loading control, at room temperature for 2 h. Subsequently, the membrane was washed, incubated with the horseradish peroxidase-conjugated goat anti-rabbit secondary antibody (Proteintech, Wuhan, China) for 1 h at room temperature, and exposed using the ECL kit.

Techniques: Expressing, Control, Western Blot