Hydrophobic interaction chromatography of fibroblast proteoglycans
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1107237
- author
- Schmidtchen, Artur LU and Fransson, Lars-Åke LU
- organization
- publishing date
- 1993
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biomedical Chromatography
- volume
- 7
- issue
- 1
- pages
- 48 - 55
- publisher
- John Wiley & Sons Inc.
- 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
- 2016-04-01 16:34:36
- date last changed
- 2021-01-03 11:00:39
@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 Inc.}},
series = {{Biomedical Chromatography}},
title = {{Hydrophobic interaction chromatography of fibroblast proteoglycans}},
url = {{http://dx.doi.org/10.1002/bmc.1130070113}},
doi = {{10.1002/bmc.1130070113}},
volume = {{7}},
year = {{1993}},
}