Abstract
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 pH 3.40, 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 NaCI gradient (0→1.0M) elution at pH 7.30.
