title: SAXS studies of human protein HC (alpha1-microglobulin).
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 (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)=6.3 nm and the dimer by R(G)=2.99 nm and D(max)=9.5 nm.
authors.affiliation: Department of Macromolecular Physics, Adam Mickiewicz University, Poznan, Poland. mkozak@amu.edu.pl
authors.forename: M
authors.initials: M
authors.lastname: Kozak
authors.forename: A
authors.initials: A
authors.lastname: Grubb
mesh_terms: D000510:Alpha-Globulins / Q000737:chemistry* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008958:Models, Molecular; D053838:Scattering, Small Angle; D014961:X-Ray Diffraction / Q000379:methods*
chemical_list: D000510:Alpha-Globulins; C016001:alpha-1-microglobulin