SAXS Studies of Human Protein HC (α1-Microglobulin)

Title: SAXS Studies of Human Protein HC (α1-Microglobulin)

Volume: 14 Issue: 5

Author(s): M. Kozak and A. Grubb

Affiliation:

Keywords: solution scattering, synchrotron radiation, protein hc, glycoprotein, small angle x-ray scattering

Abstract: 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 (λ=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 RG= 2.20 nm and Dmax=6.3 nm and the dimer by RG=2.99 nm and Dmax=9.5 nm.

Cite this article as:

Kozak M. and Grubb A., SAXS Studies of Human Protein HC (α1-Microglobulin), Protein & Peptide Letters 2007; 14 (5) . https://dx.doi.org/10.2174/092986607780782830

DOI https://dx.doi.org/10.2174/092986607780782830	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305