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Hydrophobic interaction chromatography of fibroblast proteoglycans

Schmidtchen, Artur LU and Fransson, Lars-Åke LU (1993) In Biomedical Chromatography 7(1). p.48-55
Abstract
We have investigated the hydrophobic properties of human skin fibroblast proteoglycans and related material by affinity chromatography on Octyl-Sepharose CL-4B in 4 M guanidinium hydrochloride (GdnHCl). Proteoglycans and related material could be separated into non-, medium and highly hydrophobic forms by elution with gradients of Triton X-100 in 4 M Gdn HCl. The non-hydrophobic material included endogenously produced glycosaminoglycan chains and oligosaccharides as well as an HS-proteoglycan with a 35 kDa core. The 65-70 kDa core (glypican-related) proteoglycans appeared among the highly hydrophobic ones, but variable proportions were seen both in the medium and the non-hydrophobic material. Other membrane-bound proteoglycans, like... (More)
We have investigated the hydrophobic properties of human skin fibroblast proteoglycans and related material by affinity chromatography on Octyl-Sepharose CL-4B in 4 M guanidinium hydrochloride (GdnHCl). Proteoglycans and related material could be separated into non-, medium and highly hydrophobic forms by elution with gradients of Triton X-100 in 4 M Gdn HCl. The non-hydrophobic material included endogenously produced glycosaminoglycan chains and oligosaccharides as well as an HS-proteoglycan with a 35 kDa core. The 65-70 kDa core (glypican-related) proteoglycans appeared among the highly hydrophobic ones, but variable proportions were seen both in the medium and the non-hydrophobic material. Other membrane-bound proteoglycans, like fibroglycan (45 kDa core) and the HS-proteoglycans with 90 and 130 kDa cores, as well as the CS/DS-proteoglycan with a 90 kDa core, were all of high hydrophobicity. There were also indications of a highly hydrophobic CS/DS-proteoglycan with a 45 kDa core. The extracellular proteoglycans, PG-L, PG-S1 and PG-S2, and the HS-proteoglycans with 350 and 250 kDa cores were all of medium hydrophobicity. These proteoglycans emerged in distinct positions when the column was eluted with a gradient of 3-[(3-cholamidopropyl)dimethylammonio]propanesulphonate. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biomedical Chromatography
volume
7
issue
1
pages
48 - 55
publisher
John Wiley & Sons
external identifiers
  • pmid:8431681
  • scopus:0027469697
ISSN
0269-3879
DOI
10.1002/bmc.1130070113
language
English
LU publication?
yes
id
6dc25fbe-56e5-48c1-9b10-f08d8ac83785 (old id 1107237)
date added to LUP
2008-07-30 14:24:27
date last changed
2017-01-01 07:09:02
@article{6dc25fbe-56e5-48c1-9b10-f08d8ac83785,
  abstract     = {We have investigated the hydrophobic properties of human skin fibroblast proteoglycans and related material by affinity chromatography on Octyl-Sepharose CL-4B in 4 M guanidinium hydrochloride (GdnHCl). Proteoglycans and related material could be separated into non-, medium and highly hydrophobic forms by elution with gradients of Triton X-100 in 4 M Gdn HCl. The non-hydrophobic material included endogenously produced glycosaminoglycan chains and oligosaccharides as well as an HS-proteoglycan with a 35 kDa core. The 65-70 kDa core (glypican-related) proteoglycans appeared among the highly hydrophobic ones, but variable proportions were seen both in the medium and the non-hydrophobic material. Other membrane-bound proteoglycans, like fibroglycan (45 kDa core) and the HS-proteoglycans with 90 and 130 kDa cores, as well as the CS/DS-proteoglycan with a 90 kDa core, were all of high hydrophobicity. There were also indications of a highly hydrophobic CS/DS-proteoglycan with a 45 kDa core. The extracellular proteoglycans, PG-L, PG-S1 and PG-S2, and the HS-proteoglycans with 350 and 250 kDa cores were all of medium hydrophobicity. These proteoglycans emerged in distinct positions when the column was eluted with a gradient of 3-[(3-cholamidopropyl)dimethylammonio]propanesulphonate.},
  author       = {Schmidtchen, Artur and Fransson, Lars-Åke},
  issn         = {0269-3879},
  language     = {eng},
  number       = {1},
  pages        = {48--55},
  publisher    = {John Wiley & Sons},
  series       = {Biomedical Chromatography},
  title        = {Hydrophobic interaction chromatography of fibroblast proteoglycans},
  url          = {http://dx.doi.org/10.1002/bmc.1130070113},
  volume       = {7},
  year         = {1993},
}