Kee Min Woo , Woelsung Yi , Young Jong Sohn , Chung-Soon Chang , Man-Sik Kang , Doo Bong Ha , Chin Ha Chung
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Purification and characterization of a poly-l-lysine-activated serine endoprotease from Lumbricus rubellus
An endoprotease in earthworm (Lumbricus rubellus) is purified to apparent homogeneity using 125I-lactalbumin as a substrate. The protease has a molecular mass of 27 kDa and is markedly activated by poly-l-lysine or poly-l-arginine. It is a chymotrypsin-like serine protease. Its activity is distributed to coelomic fluid but relatively little to coelomocytes.
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