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Hydrophobic interaction chromatography of fibroblast proteoglycans

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Author

Summary, in English

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.

Publishing year

1993

Language

English

Pages

48-55

Publication/Series

Biomedical Chromatography

Volume

7

Issue

1

Document type

Journal article review

Publisher

John Wiley & Sons Inc.

Topic

  • Medicinal Chemistry
  • Dermatology and Venereal Diseases

Status

Published

Research group

  • Glycobiology

ISBN/ISSN/Other

  • ISSN: 0269-3879