Abstract
A new method for the purification of phospholipase-C (phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3) from Bacillus cereus has been developed, based on its affinity to 2-(4-aminophenylsulphonyl)ethyl derivative of beaded cellulose. The enzyme was adsorbed on the affinity sorbent through a site(s) that was clearly distinct from its catalytically active site, because it was still active in the immobilized state. A possible role of enzyme-inhibitor interaction in enzyme binding to the ligand used is discussed.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adsorption
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Bacillus cereus / enzymology*
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Binding Sites
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Cellulose / analogs & derivatives*
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Chromatography, Affinity*
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Hydrogen-Ion Concentration
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Kinetics
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Phosphorylcholine / analogs & derivatives
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Phosphorylcholine / metabolism
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Sulfathiazole
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Sulfathiazoles / pharmacology
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Tromethamine / pharmacology
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Type C Phospholipases / antagonists & inhibitors
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Type C Phospholipases / isolation & purification*
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Type C Phospholipases / metabolism
Substances
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4-nitrophenylphosphorylcholine
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Sulfathiazoles
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Tromethamine
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Phosphorylcholine
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2-(4-aminophenylsulfonyl)ethyl cellulose
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Cellulose
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Type C Phospholipases
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Sulfathiazole