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Image Search Results
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
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
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
Techniques: Glycoproteomics, Filtration