Purification and characterization of phospholipase C of Salmonella gallinarum.
Phospholipase C was isolated from an outbreak strain of Salmonella gallinarum with ciprofloxacin extraction, dialysis, gel filtration, ion exchange chromatography and chromatofocussing. Purified phospholipase C (mol wt. 65 KDa; isoelectric point, pI 3.5) was resistant to pasteurization, stomach enzyme (pepsin), bacterial protease and lipase but lost its activity on trypsin and chymotrypsin treatment. It was sensitive to pH > or = 8.0. It was haemolytic, embryotoxic, enterohaemorrhagic, lethal to birds, cytotoxic to Vero and MDBK cells, dermonecrotoxic in rabbit and antigenically active protein. Antisera raised against purified phospholipase C neutralized its all biological activities and agglutinated the producer Salmonella strains. Serologically it was proved similar to phospholipase C of Klebsiella pneumoniae and S. weltevreden. Fluorescent antibody technique (FAT) was standardized to detect phospholipase producer strains.
Singh
B R
BR
Department of Veterinary Microbiology, College of Veterinary Sciences, GB Pant University of Agriculture and Technology, Pantnagar, India.
Sharma
V D
VD
D000818:Animals; D002460:Cell Line; D002470:Cell Survival / Q000187:drug effects; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007928:Lethal Dose 50; D012475:Salmonella / Q000201:enzymology*; D010738:Type C Phospholipases / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology
D010738:Type C Phospholipases