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Purification and kinetics of extracellular phospholipase a ofSalmonella newport

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Abstract

Attempts were made to purify and study the kinetics of extracellular phospholipase A ofSalmonella newport (6,8, eb; 1,2). The enzyme was purified by salt precipitation followed by gel filtration, using different grades of Sephadex. The enzymically active purified preparation was found to be a protein, having molar mass ranging between 43 and 67 kDa. The enzyme had a pH optimum at 7.5, giving 18.2 μg of lysophosphatidylcholine per mg protein. Its activity was enhanced by all metal ions except potassium, by solvents and surfactants except sodium dodecyl sulfate. It hydrolyzed the membrane phospholipids of red blood cells and was inhibitory to the growth of other microorganisms.

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Neena, S., Asnani, P.J., Bhandari, S. et al. Purification and kinetics of extracellular phospholipase a ofSalmonella newport . Folia Microbiol 37, 205–209 (1992). https://doi.org/10.1007/BF02933148

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