Multiple extracellular phospholipase activities from Prevotella intermedia.
Enzyme preparations obtained from Prevotella intermedia culture supernatants were partially purified by ammonium sulfate precipitation and ion-exchange column chromatography. Hydrolytic activities were revealed by an assay that uses silicic acid thin layer chromatography to separate the products derived from (14)C-labeled phosphatidyl-choline (PC) hydrolysis. These products were then measured by liquid scintillation spectrometry after iodine visualization. The assays revealed linearity of substrate depletion and product formation with respect to time and protein concentration up to 30 min of incubation. The products had retention times consistent with lyso-phospholipids and phosphoryl-choline. These data strongly suggests the presence of both phospholipase A (PL-A) and phospholipase C (PL-C) activities.
Bulkacz
Jaime
J
Section of Periodontics, UCLA School of Dentistry, USA. Jbulkacz@ucla.edu
Faull
Kym F
KF
D001426:Bacterial Proteins / Q000302:isolation & purification*; D002250:Carbon Radioisotopes / Q000378:metabolism; D005591:Chemical Fractionation; D002852:Chromatography, Ion Exchange; D003470:Culture Media / Q000737:chemistry*; D007700:Kinetics; D010713:Phosphatidylcholines / Q000378:metabolism; D010740:Phospholipases / Q000302:isolation & purification*; D018713:Prevotella intermedia / Q000201:enzymology*
D001426:Bacterial Proteins; D002250:Carbon Radioisotopes; D003470:Culture Media; D010713:Phosphatidylcholines; D010740:Phospholipases