SAXS studies of human protein HC (α1-microglobulin)

被引:2
|
作者
Kozak, M.
Grubb, A.
机构
[1] Adam Mickiewicz Univ Poznan, Dept Macromol Phys, PL-61614 Poznan, Poland
[2] Univ Hosp, Dept Clin Chem, Lund, Sweden
来源
PROTEIN AND PEPTIDE LETTERS | 2007年 / 14卷 / 05期
关键词
solution scattering; synchrotron radiation; protein HC; glycoprotein; small angle X-ray scattering;
D O I
10.2174/092986607780782830
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein HC is a low molecular weight heterogeneous glycoprotein widely distributed in human body fluids and belonging to the lipocalin superfamily. The monomer contains a single (183 amino acid residues long) peptide chain with 3 cysteine residues (2 of which form a disulfide bridge) and is glycosylated. The molecular mass of the glycosylated protein is about 27 kDa. Native gel electrophoresis results revealed partial oligomerisation of protein HC, which therefore was analysed by gel filtration. Two forms (monomer and dimer) of the protein HC were isolated. The SAXS data were recorded on an X33 camera using synchrotron radiation (lambda=0.15 nm) at X33 beamline at the DORIS storage ring of DESY (Hamburg, Germany). Solution scattering results permitted determination of the structural parameters of both forms of the protein studied. The monomer of protein HC is characterised by a radius of gyration R-G = 2.20 nm and D-max =63 nm and the dimer by R-G=2.99 nm and D-max = 9.5 nm.
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页码:425 / 429
页数:5
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