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Heterogeneity of heparan sulfate proteoglycans synthesized by PYS-2 cells.

Abstract
Antibodies to the basement membrane proteoglycan produced by the EHS tumor were used to immunoprecipitate [35S]sulfate-labeled protoglycans produced by PYS-2 cells. The immunoprecipitated proteoglycans were subsequently fractionated by CsCl density gradient centrifugation and Sepharose CL-4B chromatography. The culture medium contained a low-density proteoglycan eluting from Sepharose CL-4B at Kav = 0.18, containing heparan sulfate side chains of Mr = 35-40,000. The medium also contained a high-density proteoglycan eluting from Sepharose CL-4B at Kav = 0.23, containing heparan sulfate side chains of Mr = 30,000. The corresponding proteoglycans of the cell layer were all smaller than those in the medium. Since the antibodies used to precipitate those proteoglycans were directed against the protein core, this suggests that these proteoglycans share common antigenic features, and may be derived from a common precursor which undergoes modification by the removal of protein segments and a portion of each heparan sulfate chain.
AuthorsB Tyree, E A Horigan, D L Klippenstein, J R Hassell
JournalArchives of biochemistry and biophysics (Arch Biochem Biophys) Vol. 231 Issue 2 Pg. 328-35 (Jun 1984) ISSN: 0003-9861 [Print] United States
PMID6233937 (Publication Type: Journal Article)
Chemical References
  • Glycosaminoglycans
  • Proteoglycans
  • Heparitin Sulfate
Topics
  • Animals
  • Cell Line
  • Centrifugation, Density Gradient
  • Chemical Precipitation
  • Chromatography, Gel
  • Dysgerminoma
  • Glycosaminoglycans
  • Heparitin Sulfate (analogs & derivatives, biosynthesis)
  • Immunochemistry
  • Mice
  • Proteoglycans (biosynthesis)

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