Expression of a functional proteinase inhibitor capable of accepting xylose: bikunin

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Abstract

Bikunin is a Kunitz-type proteinase inhibitor, which is cross-linked to heavy chains via a chondroitin sulfate chain, forming inter-alpha-inhibitor and related molecules. Rat bikunin was produced by baculovirus-infected insect cells. The protein could be purified with a total yield of 20 mg/liter medium. Unlike naturally occuring bikunin the recombinant protein had no galactosaminoglycan chain. Endoglycosidase digestion also suggested that the recombinant form lacked N-linked oligosaccharides. Bikunin is translated as a part of a precursor, alpha1-microglobulin/bikunin, but the functional significance of the cotranslation is unknown. Our results indicate that the proteinase inhibitory function of bikunin is not regulated by the alpha1-microglobulin-part of the alpha1-microglobulin/bikunin precursor since recombinant bikunin had the same trypsin inhibitory activity as the recombinant precursor. Both free bikunin and the precursor were also functional as a substrate in an in vitro xylosylation system. This demonstrates that the alpha1-microglobulin-part is not necessary for the first step of galactosaminoglycan assembly.

Detaljer

Författare
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Infektionsmedicin
  • Cancer och onkologi
  • Cell- och molekylärbiologi
  • Immunologi inom det medicinska området

Nyckelord

Originalspråkengelska
Sidor (från-till)99-106
TidskriftArchives of Biochemistry and Biophysics
Volym387
Utgåva nummer1
StatusPublished - 2001
PublikationskategoriForskning
Peer review utfördJa