Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

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

Författare

Summary, in English

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.

Publiceringsår

2007

Språk

Engelska

Sidor

425-429

Publikation/Tidskrift/Serie

Protein Peptide Letters

Volym

14

Issue

5

Dokumenttyp

Artikel i tidskrift

Förlag

Bentham Science Publishers

Ämne

  • Pharmacology and Toxicology
  • Medicinal Chemistry

Nyckelord

  • glycoprotein
  • protein HC
  • solution scattering
  • synchrotron radiation
  • small angle X-ray scattering.

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 0929-8665