Human Eosinophil Major Basic Protein 2: Location of Disulfide Bonds and Free Sulfhydryl Groups

被引:0
|
作者
Lori A. Wagner
Lyo E. Ohnuki
Krishna Parsawar
Gerald J. Gleich
Chad C. Nelson
机构
[1] University of Utah,Department of Dermatology, School of Medicine
[2] University of Utah,Mass Spectrometry and Proteomics Core Facility
[3] University of Utah,Department of Medicine, School of Medicine
来源
The Protein Journal | 2007年 / 26卷
关键词
Eosinophil; major basic protein; disulfide bonds; C-type lectin;
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学科分类号
摘要
Eosinophil granule major basic protein 2 (MBP2 or major basic protein homolog) is a paralog of major basic protein (MBP1) and, similar to MBP1, is cytotoxic and cytostimulatory in vitro. MBP2, a small protein of 13,433 Da molecular weight, contains 10 cysteine residues. Mass spectrometry shows two cystine disulfide linkages (Cys20–Cys115 and Cys92–Cys107) and 6 cysteine residues with free sulfhydryl groups (Cys2, Cys23, Cys42, Cys43, Cys68, and Cys96). MBP2, similar to MBP1, has conserved motifs in common with C-type lectins. The disulfide bond locations are conserved among human MBP1, MBP2 and C-type lectins.
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页码:13 / 18
页数:5
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