Isolation and Properties of the Insoluble Collagen Fraction from Bovine Nasal Septal Cartilage

The insoluble collagen fraction (ICF) was prepared from bovine nasal cartilage by aqueous extraction (Schubert's method), followed by extraction with 8m urea in 1M NaCl. The amino acid composition of the ICF was very similar to that of the soluble cartilage collagen ever reported, but the ICF c...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1973-09, Vol.74 (3), p.505-511
Main Authors: HANADA, Eisuke, ANAN, F.K.
Format: Article
Language:English
Subjects:
Amino Acids - analysis
Animals
Cartilage - analysis
Cattle
Chondroitin - analysis
Chromatography
Collagen - isolation & purification
Glycosaminoglycans - analysis
Hexosamines - analysis
Hexoses - analysis
Hydrogen-Ion Concentration
Hydroxyproline - analysis
Nasal Septum - analysis
Neuraminic Acids - analysis
Solubility
Uronic Acids - analysis
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Summary:The insoluble collagen fraction (ICF) was prepared from bovine nasal cartilage by aqueous extraction (Schubert's method), followed by extraction with 8m urea in 1M NaCl. The amino acid composition of the ICF was very similar to that of the soluble cartilage collagen ever reported, but the ICF contained small amounts of hexuronic acid, hexose, hexosamine, and sialic acid. The ICF in the particle form was shown to bind chondroitin sulfate C (ChS-C) at pH3.40, and to a lesser extent, at pH 7.30. The similar binding of cartilage acid glycosaminoglycan and proteoglycan with ICF was also demonstrated. An ICF column which adsorbed ChS-C at pH 3.40 exhibited one peak by pH gradient elution between pH 3.40 and 7.30, and another peak by NaCl gradient (O→1.0 M) elution at pH 7.30.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a130270