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

Falkenberg, Cecilia LU ; Wester Rosenlöf, Lena LU ; Belting, Mattias LU ; Eklund, Erik LU and Åkerström, Bo LU (2001) In Archives of Biochemistry and Biophysics 387(1). p.99-106
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... (More)
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. (Less)
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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
bikunin, greek small letter alpha1-microglobulin/bikunin precursor, proteinase inhibition, xylosylation, insect cells
in
Archives of Biochemistry and Biophysics
volume
387
issue
1
pages
99 - 106
publisher
Academic Press
external identifiers
  • pmid:11368189
  • scopus:0035263886
ISSN
0003-9861
DOI
10.1006/abbi.2000.2213
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Oncology, MV (013035000), Medical Inflammation Research (013212019), Matrix biology (013212025), Division of Infection Medicine (BMC) (013024020), Department of Experimental Medical Science (013210000)
id
531c46e9-e55e-4411-9f92-81efb580bcae (old id 1121578)
date added to LUP
2016-04-01 12:02:45
date last changed
2022-01-26 22:01:48
@article{531c46e9-e55e-4411-9f92-81efb580bcae,
  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.}},
  author       = {{Falkenberg, Cecilia and Wester Rosenlöf, Lena and Belting, Mattias and Eklund, Erik and Åkerström, Bo}},
  issn         = {{0003-9861}},
  keywords     = {{bikunin; greek small letter alpha1-microglobulin/bikunin precursor; proteinase inhibition; xylosylation; insect cells}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{99--106}},
  publisher    = {{Academic Press}},
  series       = {{Archives of Biochemistry and Biophysics}},
  title        = {{Expression of a functional proteinase inhibitor capable of accepting xylose: bikunin}},
  url          = {{http://dx.doi.org/10.1006/abbi.2000.2213}},
  doi          = {{10.1006/abbi.2000.2213}},
  volume       = {{387}},
  year         = {{2001}},
}