Purification and Partial Characterization of Human C1-Esterase |
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Authors: | Hiroyuki Sumi Mutsumi Muramatu |
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Affiliation: | 1. Institute for Enzyme Research, School of Medicine, Tokushima University, Tokushima, Japan;2. Department of Pharmacy, Tokushima University of Art and Science, Tokushima, Japan |
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Abstract: | C1-Esterase was purified from the euglobulin fraction of human plasma by successive column chromatography on DEAE-cellulose, hydroxylapatite and TEAE-cellulose. The final product, purified 3500-fold with respect to serum, hydrolyzed 1,155 μmoles of Nα-acetyl-l-tyrosine ethyl ester per milligram of protein at pH 7.4 and 37°C in 15 min. The homogeneity of the purified C1-esterase was confirmed by ultracentrifugation and disc-electrophoresis. Its s20,w value was 4.3 and its molecular weight was determined as 113,000 by gel filtration on Sephadex G–200.Cl-Esterase possesses esterolytic activity for both Nα-acetyl-l-tyrosine ethyl ester and Nα-tosyl-l-arginine methyl ester, and acts on human kininogen I and II releasing kinin very slowly. |
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Keywords: | Pseudomonas aeruginosa membrane vesicles phospholipid fatty acid |
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