Expression of a functional proteinase inhibitor capable of accepting xylose: bikunin
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1121578
- author
- Falkenberg, Cecilia LU ; Wester Rosenlöf, Lena LU ; Belting, Mattias LU ; Eklund, Erik LU and Åkerström, Bo LU
- organization
- publishing date
- 2001
- 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
- 2021-01-06 08:38:05
@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},
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},
}