Carbon 13 nuclear magnetic resonance study of chondroitin 4 sulfate in the proteoglycan of bovine nasal cartilage

Curtis F. Brewer, H. Keiser

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

The Fourier transform 13C nuclear magnetic resonance spectra of bovine nasal cartilage proteoglycan subunit and complex and whole bovine nasal cartilage were obtained and compared wih that of chondroitin 4 sulfate. The spectrum of chondroitin 4 sulfate in solution revealed multiple resolvable resonances with linewidths that are consistent with considerable segmental motion in the polysaccharide chain. The spectra of proteoglycan subunit and complex in solution and that of whole cartilage were very similar to that of free chondroitin 4 sulfate chains. This indicates that the linkage of multiple chondroitin sulfate chains to proteoglycan core protein and the association of proteoglycan with collagen and other constituents of cartilage matrix does not significantly alter the structure and motions of these chains.

Original languageEnglish (US)
Pages (from-to)3421-3423
Number of pages3
JournalProceedings of the National Academy of Sciences of the United States of America
Volume72
Issue number9
StatePublished - 1975

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Nasal Cartilages
Chondroitin Sulfates
Proteoglycans
Magnetic Resonance Spectroscopy
Carbon
Cartilage
Fourier Analysis
Polysaccharides
Collagen
chondroitin sulfate proteoglycan 4
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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abstract = "The Fourier transform 13C nuclear magnetic resonance spectra of bovine nasal cartilage proteoglycan subunit and complex and whole bovine nasal cartilage were obtained and compared wih that of chondroitin 4 sulfate. The spectrum of chondroitin 4 sulfate in solution revealed multiple resolvable resonances with linewidths that are consistent with considerable segmental motion in the polysaccharide chain. The spectra of proteoglycan subunit and complex in solution and that of whole cartilage were very similar to that of free chondroitin 4 sulfate chains. This indicates that the linkage of multiple chondroitin sulfate chains to proteoglycan core protein and the association of proteoglycan with collagen and other constituents of cartilage matrix does not significantly alter the structure and motions of these chains.",
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T1 - Carbon 13 nuclear magnetic resonance study of chondroitin 4 sulfate in the proteoglycan of bovine nasal cartilage

AU - Brewer, Curtis F.

AU - Keiser, H.

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N2 - The Fourier transform 13C nuclear magnetic resonance spectra of bovine nasal cartilage proteoglycan subunit and complex and whole bovine nasal cartilage were obtained and compared wih that of chondroitin 4 sulfate. The spectrum of chondroitin 4 sulfate in solution revealed multiple resolvable resonances with linewidths that are consistent with considerable segmental motion in the polysaccharide chain. The spectra of proteoglycan subunit and complex in solution and that of whole cartilage were very similar to that of free chondroitin 4 sulfate chains. This indicates that the linkage of multiple chondroitin sulfate chains to proteoglycan core protein and the association of proteoglycan with collagen and other constituents of cartilage matrix does not significantly alter the structure and motions of these chains.

AB - The Fourier transform 13C nuclear magnetic resonance spectra of bovine nasal cartilage proteoglycan subunit and complex and whole bovine nasal cartilage were obtained and compared wih that of chondroitin 4 sulfate. The spectrum of chondroitin 4 sulfate in solution revealed multiple resolvable resonances with linewidths that are consistent with considerable segmental motion in the polysaccharide chain. The spectra of proteoglycan subunit and complex in solution and that of whole cartilage were very similar to that of free chondroitin 4 sulfate chains. This indicates that the linkage of multiple chondroitin sulfate chains to proteoglycan core protein and the association of proteoglycan with collagen and other constituents of cartilage matrix does not significantly alter the structure and motions of these chains.

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