Journal
PHYTOCHEMISTRY
Volume 65, Issue 11, Pages 1575-1588Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.phytochem.2004.03.031
Keywords
Arachis hypogaea; cationic peanut peroxidase; electrospray ionization mass spectrometry; tandem mass spectrometry; LC MS/MS; proteomics; glycobiology; glycomics; glycans; glycopeptides
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Cationic peanut peroxidase (CP) was isolated from peanut (Arachis hypogaea) cell suspension culture medium. CP is a glycoprotein with three N-linked glycan sites at Asn60, Asn144, and Asn185. ESI-MS of the intact purified protein reveals the microheterogeneity of the glycans. Tryptic digestion of CP gave a near complete sequence coverage by ESI-MS. The glycopeptides from the tryptic digestion were separated by RP HPLC identified by ESI-MS and the structure of the glycan chains determined by ESI-MS/MS. The glycans are large structures of up to 16 sugars, but most of their non-reducing ends have been modified giving a mixture of shorter chains at each site. Good agreement was found with the one glycan previously analyzed by H-1 NMR. This work is the basis for the future studies on the role of the glycans on stability and folding of CP and is another example of a detailed structural characterization of complex glycoproteins by mass spectrometry. (C) 2004 Elsevier Ltd. All rights reserved.
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