Abstract
Summary
Agar-gel electrophoresis shows that synovia! fluid alkaline phosphatase migrates differently from that of serum but similar to the enzyme of fresh cartilage and bone extracts. It is concluded that the syn-ovial fluid enzyme is derived from the articulating cartilage and not from serum. Purification of the synovial fluid enzyme by a method involving chromatography on TEAE-cellu-lose leads to modification of the enzyme that is accompanied by a change in electrophoretic mobility but not in its rate of sedimentation in a sucrose gradient. Changes in mobility of phosphatases occurred as the result of aging cartilage extracts or treating synovial fluid with neuraminidase. Chymotrypsin and trypsin, which do not alter the mobility, inactivate the phosphatase of cartilage.
We thank Dr. Ben Moffett and Miss Janice Ruffing for performing the histological studies.
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