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  • Title: Purification and characterization of a serine proteinase inhibitor from human articular cartilage.
    Author: Burkhardt H, Kasten M, Rauls S.
    Journal: Biochim Biophys Acta; 1987 May 19; 924(2):312-8. PubMed ID: 3494475.
    Abstract:
    An inhibitor of serine proteinases from human articular cartilage was purified to homogeneity by sequential ultrafiltration and ion exchange chromatography on CM-Sephadex C-50. The apparent molecular weight of the cationic glycoprotein (pI greater than 10) was determined to be 16.5 X 10(3) by SDS gel electrophoresis. The inhibitor blocked the activity of leukocyte elastase, cathepsin G and trypsin but not leukocyte collagenase. In kinetic studies for the interactions with leukocyte elastase a firm enzyme-inhibitor binding was obtained. Amino acid analyses did not reveal homologies with other serine proteinase inhibitors already purified from human tissues.
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