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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/647969
- author
- Kozak, M.
and Grubb, Anders
LU
- organization
- publishing date
- 2007
- 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
- 2016-04-01 11:57:19
- date last changed
- 2023-01-03 01:47:53
@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}},
keywords = {{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}},
doi = {{10.2174/092986607780782830}},
volume = {{14}},
year = {{2007}},
}