2009
DOI: 10.1016/j.plaphy.2008.10.005
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A small-scale method for the preparation of plant N-linked glycans from soluble proteins for analysis by MALDI-TOF mass spectrometry

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Cited by 17 publications
(5 citation statements)
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“…Thus, it can be essential in some instances to characterize the sugar moieties of recombinantly expressed proteins in detail to assess product consistency as well as to understand the relationship between glycan structure and function. Several methods have been described for detailed characterization of the glycan profiles of proteins, ranging from HPLC over capillary electrophoresis to MS‐based methods [94].…”
Section: Quality‐control Criteria and Methodologies Appliedmentioning
confidence: 99%
“…Thus, it can be essential in some instances to characterize the sugar moieties of recombinantly expressed proteins in detail to assess product consistency as well as to understand the relationship between glycan structure and function. Several methods have been described for detailed characterization of the glycan profiles of proteins, ranging from HPLC over capillary electrophoresis to MS‐based methods [94].…”
Section: Quality‐control Criteria and Methodologies Appliedmentioning
confidence: 99%
“…N -glycans were prepared and purified from the mutant and wild-type rice leaves according to Karg et al [ 55 ]. The N -glycan analysis was performed in positive-ion reflectron mode using a matrix-assisted laser desorption ionization-time of flight mass spectrometer (MALDI-TOF MS) with an Autoflex system from Bruker Daltonics (Bruker, Billerica, MA, USA).…”
Section: Methodsmentioning
confidence: 99%
“…In general, PNGase A and F are available to release N-glycans. However, PNGase F cannot release N-glycans containing α1,3-linked Fuc from proteins (Karg et al, 2009), but PNGase A can cleave α 1,3-linked Fuc. Further treatment with PNGase A and F could enzymatically release the N-glycans of okra glycoprotein.…”
Section: Characterisation Of N-glycan Structure By Maldi-tof-msmentioning
confidence: 99%