Studies on the composition of the extracellular fluid from calf costal cartilage

• Published in: Biochimica et biophysica acta Vol. 230; no. 3; pp. 620 - 626
• Main Authors: Rabadjija, Luka, Koren, Eugen, Pende, Berislav
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.01.1971
• Subjects: Animals; Cartilage - analysis; Cartilage - enzymology; Cattle; Charcoal; Chlorides - analysis; Chlorides - blood; Chromatography, Ion Exchange; Collagen - isolation & purification; Extracellular Space - analysis; Extracellular Space - enzymology; Hydroxyproline - analysis; Hydroxyproline - blood; Microbial Collagenase - analysis; Microbial Collagenase - blood; Peptide Hydrolases - analysis; Peptide Hydrolases - blood; Peptide Hydrolases - isolation & purification; Potassium - analysis; Potassium - blood; Proline - analysis; Ribs - analysis; Ribs - enzymology; Sodium - analysis; Sodium - blood; Spectrophotometry
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(71)90196-6

Appreciable amounts of free and bound hydroxyproline were found in the tissue fluid obtained by centrifugation from calf costal cartilage. In the tissue fluid the presence of an enzyme capable of splitting synthetic collagenase substrate at pH 7.4 and 37° was also demonstrated. The enzyme has been partially purified by (NH 4 2SO 4 saturation. Peak activity was obtained in the fraction of 50–60% saturation. The enzyme was not capable of degrading insoluble bovine. Achilles tendon collagen. In our opinion the enzyme cannot be considered a collagenase, and we call its activity “collagenase-like peptidase activity”.