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Proteoglycans of hyaline cartilage. Electron microscopic studies on isolated molecules

Thyberg, J. ; Lohmander, S. LU orcid and Heinegard, D. (1975) In Biochemical Journal 151(1). p.157-166
Abstract

Proteoglycan monomers from guinea pig costal cartilage, bovine nasal and bovine tracheal cartilage were observed in the electron microscope after being spread in a monomolecular layer with cytochrome c. The proteoglycan molecule appeared as an extended central core filament to which side chain filaments were attached at various intervals. The molecules from the three sources displayed great ultrastructural similarities. On average, the core filament was about 290 nm long, there were about 25 side chain filaments per core filament, the side chain filaments were about 45 nm long, and the distance between the attachment points of the side chain filaments to the core filament was about 11 nm. With regard to overall size of the molecules, no... (More)

Proteoglycan monomers from guinea pig costal cartilage, bovine nasal and bovine tracheal cartilage were observed in the electron microscope after being spread in a monomolecular layer with cytochrome c. The proteoglycan molecule appeared as an extended central core filament to which side chain filaments were attached at various intervals. The molecules from the three sources displayed great ultrastructural similarities. On average, the core filament was about 290 nm long, there were about 25 side chain filaments per core filament, the side chain filaments were about 45 nm long, and the distance between the attachment points of the side chain filaments to the core filament was about 11 nm. With regard to overall size of the molecules, no evidence of distinct subpopulations was obtained. Good correlation was found between ultrastructural data for the proteoglycan molecules and chemical data obtained by enzyme digestions and gel chromatography. Together these data strongly support the interpretation of the electron microscopic pictures as indicating a central filament corresponding to the protein core and side chain filaments corresponding to the chondroitin sulphate chain clusters of the proteoglycan monomers.

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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical Journal
volume
151
issue
1
pages
10 pages
publisher
Portland Press
external identifiers
  • scopus:0016839230
  • pmid:174551
ISSN
0264-6021
language
English
LU publication?
yes
id
10234803-2032-4e75-b7be-04ae50396903
date added to LUP
2016-05-04 12:42:47
date last changed
2024-01-04 02:38:54
@article{10234803-2032-4e75-b7be-04ae50396903,
  abstract     = {{<p>Proteoglycan monomers from guinea pig costal cartilage, bovine nasal and bovine tracheal cartilage were observed in the electron microscope after being spread in a monomolecular layer with cytochrome c. The proteoglycan molecule appeared as an extended central core filament to which side chain filaments were attached at various intervals. The molecules from the three sources displayed great ultrastructural similarities. On average, the core filament was about 290 nm long, there were about 25 side chain filaments per core filament, the side chain filaments were about 45 nm long, and the distance between the attachment points of the side chain filaments to the core filament was about 11 nm. With regard to overall size of the molecules, no evidence of distinct subpopulations was obtained. Good correlation was found between ultrastructural data for the proteoglycan molecules and chemical data obtained by enzyme digestions and gel chromatography. Together these data strongly support the interpretation of the electron microscopic pictures as indicating a central filament corresponding to the protein core and side chain filaments corresponding to the chondroitin sulphate chain clusters of the proteoglycan monomers.</p>}},
  author       = {{Thyberg, J. and Lohmander, S. and Heinegard, D.}},
  issn         = {{0264-6021}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{157--166}},
  publisher    = {{Portland Press}},
  series       = {{Biochemical Journal}},
  title        = {{Proteoglycans of hyaline cartilage. Electron microscopic studies on isolated molecules}},
  volume       = {{151}},
  year         = {{1975}},
}