Detection, prevalence, purification and characterization of lecithinase of Klebsiella pneumoniae.
Indian J Exp Biol
;
1999 Sep; 37(9): 925-32
Article
in English
| IMSEAR
| ID: sea-57493
ABSTRACT
Lecithinase activity in Klebsiella is a rare trait as out of 208 strains of Klebsiella belonging to 3 species, viz. K. pneumoniae (168), K. planticola (29) and K. oxytoca (11), only 4 strains of K. pneumoniae produced lecithinase positive colonies on egg-yolk-agar. Although cell lysates of 16 K. pneumoniae yielded positive results for lecithinase assay on egg-yolk-agar, 19 strains were detected positive for lecithinase with ELISA using anti-lecithinase serum. Release of up to 52.12% cell-bound lecithinase could be achieved with polymyxin-B treatment at 100 micrograms/ml concentration. Purified lecithinase was determined to be a high molecular weight (70 kDa), crystalizable, anionic (pI, 3.5) protein. It possessed cytolytic, haemolytic and dermonecrotic activities but did not induce fluid accumulation in rabbit ileal loop or infant mouse guts. It was inactivated by boiling, trypsin and chymotrypsin treatment and alkaline pH. Serologically, it was related to lecithinase of Aeromonas caviae and phospholipase-C of Salmonella.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Phospholipases
/
Rabbits
/
Klebsiella pneumoniae
/
Animals
/
Mice
Type of study:
Diagnostic study
/
Prevalence study
Language:
English
Journal:
Indian J Exp Biol
Year:
1999
Type:
Article
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