期刊
JOURNAL OF MOLECULAR STRUCTURE
卷 980, 期 1-3, 页码 18-23出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molstruc.2010.06.031
关键词
Glycoprotein; Cu/Zn-superoxide dismutase; MALDI-TOF-TOF; Q-Trap; Yeast Kluyveromyces marxianus
资金
- National Science Fund, Ministry of Education and Science - Republic of Bulgaria [B201/06-2492]
The primary structure of Cu/Zn-superoxide dismutase from Kluyveromyces marxianus NBIMCC 1984 was elucidated by N-terminal sequence analysis of the intact protein and by determination of the amino acid sequences of tryptic peptides by MALDI-TOF-TOF tandem mass spectrometry. The molecular mass of one subunit of the homodimer SOD, containing 152 amino acid residues, was calculated to be 15858.3 Da while a value of 17096.63 Da was obtained by MALDI-TOF MS. This difference is explained by the presence of N-glycosylation of one linkage site, -Asn-lle/Leu-Thr-, and a glycan chain with the structure Hex(5) GIcNAc(2). Glycosylation of K. marxianus superoxide dismutase is a post-translational modification. Recent developments in mass spectrometry have enabled detailed structural analyses of covalent modifications of proteins. Therefore, in this paper, we introduce a covalent modification of Cu/Zn-SOD from K. marxianus NBIMCC 1984, by analysis of the enzymatic liberated N-glycan from the enzyme using MALDI-TOF and tandem mass spectrometry on a Q-Trap mass spectrometer. This is the first report of the structure of the oligosaccharide of a naturally-glycosylated superoxide dismutase, determined by mass spectrometry. (C) 2010 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据