Correlation of lysozyme activity with proteoglycan biosynthesis in epiphyseal cartilage.
Pig epiphyseal cartilage (proximal ulna epiphysis) previously incubated into vitro in the presence of sodium [35S]sulfate or [3H]thymidine was either analyzed by autoradiography or separated into 9 morphologically defined consecutive layers and investigated for 35S-incorporation into the guanidinium chloride-extractable proteoglycans and for lysozyme activity. The lowest 35S incorporation and lysozyme activity were determined in the zone of resting cells, but there is a consecutive increase in the rate of proteoglycan synthesis and lysozyme activity toward the diaphyseal cartilage-bone junction, with the maximum at the lower columnar cell zone and a sharp reduction of both parameters at the hypertrophic zone. The maxima of 35S incorporation and [3H]thymidine incorporation do not coincide. The guanidinium chloride-soluble proteoglycans exhibit macromolecular polydispersity. Fractions excluded from as well as retarded by Sepharose 2B gel could be separated and were detected in all zones. The results indicate a correlation of proteoglycan biosynthesis and lysozyme activity in epiphyseal cartilage.
D000818:Animals; D002356:Cartilage / Q000201:enzymology / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D004838:Epiphyses / Q000033:anatomy & histology / Q000201:enzymology / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000378:metabolism; D009113:Muramidase / Q000378:metabolism*; D011509:Proteoglycans / Q000096:biosynthesis*; D014457:Ulna
D006025:Glycosaminoglycans; D011509:Proteoglycans; D004247:DNA; D009113:Muramidase