An Arginine Specific Protease from Spirulina platensis |
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Authors: | Etsuko Yada Hiroyuki Nagata Yukinori Noguchi Yoh Kodera Hiroyuki Nishimura Yuji Inada Ayako Matsushima |
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Institution: | (1) Department of Biomedical Engineering, Toin University of Yokohama, Toin Human Science and Technology Center, 1614, Kurogane-cho, Aoba-ku Yokohama, 225-8502, Japan |
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Abstract: | An arginine specific protease, Sp-protease, was purified by column chromatography from freeze-dried Spirulina platensis using a five-step process. Purified Sp-protease has a molecular weight of 80 kDa. It hydrolyzed the synthetic substrates
containing arginine residue in the P1 position but did not hydrolyze synthetic substrates containing other amino acid residues,
including lysine residue in the P1 position. Among the synthetic substrates tested, a substrate of plasminogen activator (Pyr-Gly-Arg-MCA)
was hydrolyzed most effectively with the enzyme (Km = 5.5 × 10−6 M), and fibrin gel was solubilized via activation of intrinsic plasminogen to plasmin with the enzyme. Activity was inhibited
completely with camostat mesilate (Ki = 1.1 × 10−8 M) and leupeptin (Ki = 3.9 × 10−8 M) but was not inhibited with Nα-tosyl-L-lysine chloromethyl ketone (TLCK). The optimum pH of the enzyme has a range of pH 9.0 to pH 11.0. The optimum temperature
was 50°C; the enzyme was stable at 0–50°C. |
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Keywords: | Spirulina platensis arginine specific protease fibrinolysis plasminogen activator |
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