Purification and characterisation of 6 and 58 Kda forms of the endogenous serine proteinase inhibitory proteins of ovine articular cartilage

Walter De Gruyter & Co
Publication Type:
Journal Article
Biological Chemistry, 1996, 377 (12), pp. 837 - 845
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The major ovine articular cartilage (AC) serine proteinase inhibitory protein (SPI), a 58 kDa glycoprotein (SPI-58), was purified to homogeneity by sequential Sephacryl S-300 gel permeation, concanavalin A affinity, Mono Q anion exchange and Superose 12
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