[Lipase and phospholipase from Staphylococcus aureus of different origin. II. Purification and characterization (author's transl)].
Lipase and phospholipase C from Staphylococcus aureus could be isolated by gel filtration on Sephacryl S 200 (Fig. 1a, b) and completely separated by refiltration under the same conditions. Isoelectric focusing gave maximal enzyme-activities for lipase at pH 8.6 and 9.5 and for phospholipase C at pH 7.4 (Fig. 2). Thin-layer chromatography revealed that the reaction products in lecithin agar of the phospholipase C-preparations from S. aureus and Bacillus cereus were identical (Table 1).
D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D005260:Female; D006801:Humans; D007525:Isoelectric Focusing; D008049:Lipase / Q000302:isolation & purification*; D008414:Mastitis, Bovine / Q000382:microbiology; D010740:Phospholipases / Q000302:isolation & purification*; D013203:Staphylococcal Infections / Q000382:microbiology; D013211:Staphylococcus aureus / Q000201:enzymology*; D010738:Type C Phospholipases / Q000378:metabolism
D010740:Phospholipases; D008049:Lipase; D010738:Type C Phospholipases
Lipase und Phospholipase C von Staphylococcus aureus verschiedener Herkunft. II. Reinigung und Charakterisierung.