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- W2040395880 abstract "Abstract 1. 1. Clostridium perfringens phospholipase C (α-toxin) (EC 3.1.4.3) was extensively purified by affinity chromatography on agarose-linked egg-yolk lipoprotein, followed by gel filtration on Sephadex G-100. The purification achieved was 200-fold from crude enzyme (2500-fold from the culture filtrate) with a yield of approx. 60% with respect to either enzymatic, lethal or hemolytic activity. 2. 2. The purified enzyme was homogeneous in polyacrylamide gel electrophoresis, ultracentrifugation and immunodiffusion. The molecular weight estimated was 43 000. The purified preparation had the highest specific activity among the preparations ever reported. 3. 3. By isoelectric focusing of the purified enzyme, three major molecular forms, designated as α 0 -, α 1 - and α 2 -toxins, and several minor ones were isolated. Isoelectric points for α 0 -, α 1 - and α 2 -toxins were 5.2, 5.3 and 5.5, respectively. These multiple forms were not distinguished from each other by immunodiffusion and electrophoresis in polyacrylamide gel with or without sodium dodecylsulfate. They shared a common susceptibility to inactivation by heat and extreme pH. 4. 4. All the multiple forms isolated had phospholipase C activity towards both lecithin and sphingomyelin, as well as lethal and hemolytic activities, indicating that these three activities reside in a single entity." @default.
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- W2040395880 date "1974-05-01" @default.
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- W2040395880 title "Purification of Clostridium perfringens phospholipase C (α-toxin) by affinity chromatography on agarose-linked egg-yolk lipoprotein" @default.
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- W2040395880 doi "https://doi.org/10.1016/0005-2795(74)90074-9" @default.
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