Purification and kinetics of extracellular phospholipase A of Salmonella newport
Language English Country United States Media print
Document type Journal Article
PubMed
1505883
DOI
10.1007/bf02933148
Knihovny.cz E-resources
- MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Phospholipases A isolation & purification metabolism MeSH
- Chromatography, Gel MeSH
- Kinetics MeSH
- Salmonella enzymology MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Phospholipases A MeSH
Attempts were made to purify and study the kinetics of extracellular phospholipase A of Salmonella 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 micrograms 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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