N-glycans were characterized by MALDI-TOF/TOF-MS (UltrafleXtreme, Bruker Daltonics; Bremen, Germany). Lyophilized N-glycans were resuspended in 5 μL MW, and 1 μL of the mixture was spotted onto an MTP AnchorChip sample target and air-dried. One μL of 20 mg/mL 2,5-dihydroxybenzoic acid (DHB) in MW was spotted to recrystallize the glycans. Mass calibration was performed using peptide calibration standards (250 calibration points; Bruker). Measurements were taken in positive-ion mode and the intense ions from MS spectra were subsequently selected and subjected to MS/MS. Representative MS spectra of N-glycans with signal-to-noise ratios >3 were chose and annotated using the GlycoWorkbench program with the accuracy < 1.0 (http://code.google.com/p/glycoworkbench/ ). Relative intensities were analyzed and generated using the FlexAnalysis software program (Bruker Daltonics). Relative variation was calculated by dividing the relative intensity of a particular type of N-glycan by the sum of N-glycan relative intensity in one scan, as described previously [47 (link)].
Flexanalysis software program
Manufactured by Bruker
FlexAnalysis is a software program developed by Bruker for the analysis and processing of data obtained from various analytical instruments. The core function of FlexAnalysis is to provide users with a comprehensive set of tools for data visualization, manipulation, and interpretation.
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Lab products found in correlation
2 protocols using flexanalysis software program
1
MALDI-TOF/TOF-MS Analysis of N-Glycans
2
MALDI-TOF Analysis of Inhibited DGL
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DGL was pre-incubated for 30 min at 25 °C with a large excess of SAPRF4 (a I = 30 µg) to abolish any residual lipolytic activity. A blank experiment was performed in the absence of SAPRF4. MALDI-TOF analysis of the entire non-inhibited or inhibited DGL was carried out with a Bruker Micoflex II mass spectrometer (Daltonik, Deutchland) using a saturated solution of α-cyano-4-hydroxycinnamic acid in acidified water (0.1 % TFA) and acetonitrile (30:70 v/v) 28 . Mass spectra were acquired in the positive ion mode, using the Flex Analysis™ software program (Bruker, Daltonik, Deutchland). Protein identification was performed using the MASCOT™ version 2.2 search engine (Matrix Science, London, UK) and the NCBI protein database. Theoretical and experimental peptide mass were obtained using the BioTools™ software program (Bruker, Daltonik, Deutchland).
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