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SAXS studies of human protein HC (alpha(1)-microglobulin)

Kozak, M. and Grubb, Anders LU (2007) In Protein Peptide Letters 14(5). p.425-429
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
glycoprotein, protein HC, solution scattering, synchrotron radiation, small angle X-ray scattering.
in
Protein Peptide Letters
volume
14
issue
5
pages
425 - 429
publisher
Bentham Science Publishers
external identifiers
  • wos:000247415500003
  • scopus:34249703024
ISSN
0929-8665
DOI
10.2174/092986607780782830
language
English
LU publication?
yes
id
52d6f284-67be-47f6-ac69-5b194b374ade (old id 647969)
date added to LUP
2007-12-12 14:56:38
date last changed
2017-01-01 04:42:01
@article{52d6f284-67be-47f6-ac69-5b194b374ade,
  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 =63 nm and the dimer by R-G=2.99 nm and D-max = 9.5 nm.},
  author       = {Kozak, M. and Grubb, Anders},
  issn         = {0929-8665},
  keyword      = {glycoprotein,protein HC,solution scattering,synchrotron radiation,small angle X-ray scattering.},
  language     = {eng},
  number       = {5},
  pages        = {425--429},
  publisher    = {Bentham Science Publishers},
  series       = {Protein Peptide Letters},
  title        = {SAXS studies of human protein HC (alpha(1)-microglobulin)},
  url          = {http://dx.doi.org/10.2174/092986607780782830},
  volume       = {14},
  year         = {2007},
}