Purification and characterization of a serine proteinase inhibitor from human articular cartilage.
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.
D000596:Amino Acids / Q000032:analysis; D002358:Cartilage, Articular / Q000201:enzymology*; D056649:Cathepsin G; D002403:Cathepsins / Q000037:antagonists & inhibitors; D006801:Humans; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D011480:Protease Inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D011506:Proteins / Q000302:isolation & purification* / Q000378:metabolism; D012697:Serine Endopeptidases; D015842:Serine Proteinase Inhibitors; D014361:Trypsin Inhibitors / Q000302:isolation & purification
D000596:Amino Acids; D011480:Protease Inhibitors; D011506:Proteins; D015842:Serine Proteinase Inhibitors; D014361:Trypsin Inhibitors; D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase